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Database: UniProt/TrEMBL
Entry: A0A1B3X2P7_9FIRM
LinkDB: A0A1B3X2P7_9FIRM
Original site: A0A1B3X2P7_9FIRM 
ID   A0A1B3X2P7_9FIRM        Unreviewed;       368 AA.
AC   A0A1B3X2P7;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-SEP-2017, entry version 7.
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=BCS37_03195 {ECO:0000313|EMBL:AOH47512.1};
OS   Selenomonas sp. oral taxon 920.
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales;
OC   Selenomonadaceae; Selenomonas.
OX   NCBI_TaxID=1884263 {ECO:0000313|EMBL:AOH47512.1, ECO:0000313|Proteomes:UP000095012};
RN   [1] {ECO:0000313|EMBL:AOH47512.1, ECO:0000313|Proteomes:UP000095012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W5150 {ECO:0000313|EMBL:AOH47512.1,
RC   ECO:0000313|Proteomes:UP000095012};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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; CP017042; AOH47512.1; -; Genomic_DNA.
DR   RefSeq; WP_069180128.1; NZ_CP017042.1.
DR   EnsemblBacteria; AOH47512; AOH47512; BCS37_03195.
DR   KEGG; selt:BCS37_03195; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000095012; 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:UP000095012};
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}.
FT   DOMAIN      243    367       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     37     37       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    264    264       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     135    135       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     311    311       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      37     37       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   368 AA;  39782 MW;  EAD056A67C8C965E CRC64;
     MPSRAAWVEI DLGAIAHNYR EIRRHTRPDA KLCAVVKADA YGHGAIAVAR KAIAAGAEYL
     AVATISEAMK LREAGFTTPL LILGLTKPDS SFDIVDADLT QTVCRLDLVQ ALSAEAVAQG
     KRVKVHLAVD TGLGRIGVHP AEAAAFARAV TALPGIELEG IFSHFALADI TDKTYTMEQI
     RRFQEACDAV AAAGIAIPIR HIAESAAILD LPDVHFDMVR AGILQYGLWP SDEVTRPLHL
     RPAMKFCARI VYIKTIPPGT SIGYGRNFIA QRESRIATIS VGYADGYLRA YAGGCVEVRG
     KRAPIAGRIC MDQCMIDITD IPEAKLGDRV TLFGSETLTA DDLARLANTI SYEVLCLVSK
     HVSRIYVE
//
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