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Database: UniProt/TrEMBL
Entry: V5SDC4_9RHIZ
LinkDB: V5SDC4_9RHIZ
Original site: V5SDC4_9RHIZ 
ID   V5SDC4_9RHIZ            Unreviewed;       376 AA.
AC   V5SDC4;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-SEP-2017, entry version 30.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   ORFNames=W911_11355 {ECO:0000313|EMBL:AHB48866.1};
OS   Hyphomicrobium nitrativorans NL23.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium.
OX   NCBI_TaxID=1029756 {ECO:0000313|EMBL:AHB48866.1, ECO:0000313|Proteomes:UP000018542};
RN   [1] {ECO:0000313|EMBL:AHB48866.1, ECO:0000313|Proteomes:UP000018542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NL23 {ECO:0000313|EMBL:AHB48866.1};
RX   PubMed=24435868;
RA   Martineau C., Villeneuve C., Mauffrey F., Villemur R.;
RT   "Complete Genome Sequence of Hyphomicrobium nitrativorans Strain NL23,
RT   a Denitrifying Bacterium Isolated from Biofilm of a Methanol-Fed
RT   Denitrification System Treating Seawater at the Montreal Biodome.";
RL   Genome Announc. 2:e01165-13(2014).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01201, ECO:0000256|SAAS:SAAS00630646}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201,
CC         ECO:0000256|PIRSR:PIRSR600821-50,
CC         ECO:0000256|SAAS:SAAS00758845};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|SAAS:SAAS00630654}.
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DR   EMBL; CP006912; AHB48866.1; -; Genomic_DNA.
DR   RefSeq; WP_023787618.1; NC_022997.1.
DR   ProteinModelPortal; V5SDC4; -.
DR   EnsemblBacteria; AHB48866; AHB48866; W911_11355.
DR   KEGG; hni:W911_11355; -.
DR   PATRIC; fig|1029756.8.peg.2360; -.
DR   KO; K01775; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000018542; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_01201; Ala_racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000018542};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018542}.
FT   DOMAIN      242    372       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     43     43       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    263    263       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     141    141       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     316    316       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      43     43       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   376 AA;  38778 MW;  4A3BE878A052DBC5 CRC64;
     MTAPPDLPPG ATGVITVDLD AIADNWRALG ALVTPAECGA VVKADAYGLG AIKVVPALAR
     AGCRTFFIAT PDEAEAARRF APDARLFALD GLLPGAASVF SANDIAPVLT SLEELAVWSA
     EATRTGKRLP AGLQIDSGLN RLGLSEDDVR TLASAPARLD GIDLRLVMSH LACADDPAHP
     HNETQRSNFD RLRTLLPPTP ASLAASDGLM LGARFHYDLV RPGYALYGGQ AFQGGPTPVR
     PAVTVEARVL QVRTLSPGDP VGYSATWRAA RPTRLAVISA GYADGIARAL SASTEREGGV
     IAIHGEAAPI VGRVSMDLIT ADVTDIAAAI APGDLATLVG PGLTVEAMGQ AGGTIGYEVL
     TRLGTRFARH YVGGGG
//
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