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Database: UniProt/TrEMBL
Entry: A0A0S2YV49_9MICC
LinkDB: A0A0S2YV49_9MICC
Original site: A0A0S2YV49_9MICC 
ID   A0A0S2YV49_9MICC        Unreviewed;       399 AA.
AC   A0A0S2YV49;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-SEP-2017, entry version 13.
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=ATC04_06335 {ECO:0000313|EMBL:ALQ30217.1};
OS   Arthrobacter sp. YC-RL1.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=1652545 {ECO:0000313|EMBL:ALQ30217.1, ECO:0000313|Proteomes:UP000061913};
RN   [1] {ECO:0000313|EMBL:ALQ30217.1, ECO:0000313|Proteomes:UP000061913}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC-RL1 {ECO:0000313|EMBL:ALQ30217.1,
RC   ECO:0000313|Proteomes:UP000061913};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) 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; CP013297; ALQ30217.1; -; Genomic_DNA.
DR   RefSeq; WP_052772431.1; NZ_LCYH01000016.1.
DR   EnsemblBacteria; ALQ30217; ALQ30217; ATC04_06335.
DR   KEGG; ary:ATC04_06335; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000061913; 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:UP000061913};
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      264    390       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     55     55       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    285    285       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     152    152       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     332    332       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      55     55       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   399 AA;  42278 MW;  5B102FFDA703E310 CRC64;
     MNSEALEQSN NSAGLATPAF SPWERRAVID LSAIRNNVKQ VVDLVAPAAV MAVVKADGYG
     HGALQVATAA LEAGASWVGC AHVTEALALR KAGIEAPMLA WLHTHDTPFD DAIAAGIDLG
     VSGWDLDAIA AAAQRLQAPA RIHLKVDTGL GRNGSTMADL PGLLQRASEY QEAGLLRVVG
     IFSHLAVADE PERPETDMQL AVFDEAIALV EAAGFDLEVR HIANTPGILS RPDSHHELVR
     LGLGLYGLSP FENETPGSFG LRPAMKLVTR VANVKKVPLN QGVSYGLSYH TTAETYLGLI
     PLGYADGLPR IATGAPVTIN GKSYPVRGRI AMDQCVIDLG PDVDPADFLG VEAVIFGEGG
     QSVNTWAYAA NTINYEVVTR ISSRVPRYYI QGSWGEAGE
//
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