ID DHA_MYCTU Reviewed; 371 AA. AC P30234; O33322; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 25-NOV-2008, entry version 66. DE RecName: Full=Alanine dehydrogenase; DE EC=1.4.1.1; DE AltName: Full=40 kDa antigen; DE AltName: Full=TB43; GN Name=ald; OrderedLocusNames=Rv2780, MT2850; ORFNames=MTV002.45; OS Mycobacterium tuberculosis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1773; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 35801 / TMC 107 / Erdman; RX MEDLINE=92267644; PubMed=1587598; RA Andersen A.B., Andersen P., Ljungqvist L.; RT "Structure and function of a 40,000-molecular-weight protein antigen RT of Mycobacterium tuberculosis."; RL Infect. Immun. 60:2317-2323(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RA Singh M., Hutter B.; RT "Host-vector system for high level expression and purification of RT enzymatically active L-alanine dehydrogenase of M.tuberculosis in RT E.coli."; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete genome sequence."; RL Nature 393:537-544(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 1551 / Oshkosh; RX MEDLINE=22206494; PubMed=12218036; RX DOI=10.1128/JB.184.19.5479-5490.2002; RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., RA Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., RA Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., RA Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., RA Fraser C.M.; RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and RT laboratory strains."; RL J. Bacteriol. 184:5479-5490(2002). RN [5] RP PROTEIN SEQUENCE OF 1-21. RC STRAIN=ATCC 25618 / H37Rv; RX MEDLINE=95122409; PubMed=7822223; RA Deshpande R.G., Khan M.B., Bhat D.A., Navalkar R.G.; RT "Isolation of a 43 kDa protein from Mycobacterium tuberculosis H37Rv RT and its identification as a pyridine nucleotide transhydrogenase."; RL J. Appl. Bacteriol. 77:639-643(1994). CC -!- FUNCTION: May play a role in cell wall synthesis as L-alanine is CC an important constituent of the peptidoglycan layer. CC -!- CATALYTIC ACTIVITY: L-alanine + H(2)O + NAD(+) = pyruvate + NH(3) CC + NADH. CC -!- PATHWAY: Amino-acid degradation; L-alanine degradation via CC dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step CC 1/1. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X63069; CAA44791.1; -; Genomic_DNA. DR EMBL; U92472; AAC38804.1; -; Genomic_DNA. DR EMBL; BX842580; CAA15575.1; -; Genomic_DNA. DR EMBL; AE000516; AAK47169.1; -; Genomic_DNA. DR PIR; C70883; A43830. DR RefSeq; NP_217296.1; -. DR RefSeq; NP_337355.1; -. DR PDB; 2VHV; X-ray; 2.80 A; A/B=1-371. DR PDB; 2VHW; X-ray; 2.00 A; A/B/C/D/E/F=1-371. DR PDB; 2VHX; X-ray; 2.00 A; A/B/C/D/E/F=1-371. DR PDB; 2VHY; X-ray; 2.30 A; A/B=1-371. DR PDB; 2VHZ; X-ray; 2.04 A; A/B=1-371. DR PDB; 2VOE; X-ray; 2.60 A; A/B/C/D/E/F=1-371. DR PDB; 2VOJ; X-ray; 2.60 A; A/C/E=1-371. DR PDBsum; 2VHV; -. DR PDBsum; 2VHW; -. DR PDBsum; 2VHX; -. DR PDBsum; 2VHY; -. DR PDBsum; 2VHZ; -. DR PDBsum; 2VOE; -. DR PDBsum; 2VOJ; -. DR GeneID; 888493; -. DR GeneID; 925435; -. DR GenomeReviews; AE000516_GR; MT2850. DR GenomeReviews; AL123456_GR; Rv2780. DR KEGG; mtc:MT2850; -. DR KEGG; mtu:Rv2780; -. DR TIGR; MT2850; -. DR TubercuList; Rv2780; -. DR HOGENOM; P30234; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:InterPro. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR007698; Ala_DHase/PNT_C. DR InterPro; IPR008142; Ala_DHase/PNT_CS1. DR InterPro; IPR008143; Ala_DHase/PNT_CS2. DR InterPro; IPR007886; Ala_DHase/PNT_N. DR InterPro; IPR008141; Ala_DHase_PNT. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF01262; AlaDh_PNT_C; 1. DR Pfam; PF05222; AlaDh_PNT_N; 1. DR ProDom; PD000139; FAD_pyr_redox; 1. DR TIGRFAMs; TIGR00518; alaDH; 1. DR PROSITE; PS00836; ALADH_PNT_1; 1. DR PROSITE; PS00837; ALADH_PNT_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; NAD; KW Oxidoreductase; Secreted. FT CHAIN 1 371 Alanine dehydrogenase. FT /FTId=PRO_0000198994. FT NP_BIND 170 200 NAD (By similarity). FT ACT_SITE 96 96 Potential. FT CONFLICT 13 13 E -> EFQ (in Ref. 1; CAA44791). FT CONFLICT 123 123 A -> P (in Ref. 4; AAK47169). FT STRAND 2 5 FT HELIX 20 28 FT STRAND 32 36 FT TURN 37 40 FT HELIX 41 43 FT HELIX 47 53 FT STRAND 56 59 FT HELIX 61 67 FT STRAND 69 72 FT HELIX 79 84 FT STRAND 90 93 FT HELIX 97 99 FT HELIX 101 110 FT STRAND 113 116 FT HELIX 117 119 FT TURN 128 130 FT HELIX 131 148 FT HELIX 151 153 FT STRAND 170 174 FT HELIX 178 189 FT STRAND 193 199 FT HELIX 201 210 FT TURN 211 213 FT STRAND 214 219 FT HELIX 222 231 FT STRAND 233 237 FT HELIX 252 255 FT STRAND 263 266 FT HELIX 267 270 FT STRAND 283 285 FT STRAND 287 290 FT STRAND 293 296 FT HELIX 301 304 FT HELIX 306 335 FT HELIX 337 340 FT STRAND 343 346 FT HELIX 353 359 FT HELIX 367 370 SQ SEQUENCE 371 AA; 38713 MW; 9DF7540524DC116A CRC64; MRVGIPTETK NNEFRVAITP AGVAELTRRG HEVLIQAGAG EGSAITDADF KAAGAQLVGT ADQVWADADL LLKVKEPIAA EYGRLRHGQI LFTFLHLAAS RACTDALLDS GTTSIAYETV QTADGALPLL APMSEVAGRL AAQVGAYHLM RTQGGRGVLM GGVPGVEPAD VVVIGAGTAG YNAARIANGM GATVTVLDIN IDKLRQLDAE FCGRIHTRYS SAYELEGAVK RADLVIGAVL VPGAKAPKLV SNSLVAHMKP GAVLVDIAID QGGCFEGSRP TTYDHPTFAV HDTLFYCVAN MPASVPKTST YALTNATMPY VLELADHGWR AACRSNPALA KGLSTHEGAL LSERVATDLG VPFTEPASVL A //