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Database: UniProt/TrEMBL
Entry: J7LTW9_9MICC
LinkDB: J7LTW9_9MICC
Original site: J7LTW9_9MICC 
ID   J7LTW9_9MICC            Unreviewed;       417 AA.
AC   J7LTW9;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   28-FEB-2018, entry version 38.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   Name=alr2 {ECO:0000313|EMBL:AFR29923.1};
GN   ORFNames=ARUE_c30380 {ECO:0000313|EMBL:AFR29923.1};
OS   Arthrobacter sp. Rue61a.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=1118963 {ECO:0000313|EMBL:AFR29923.1, ECO:0000313|Proteomes:UP000003736};
RN   [1] {ECO:0000313|EMBL:AFR29923.1, ECO:0000313|Proteomes:UP000003736}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rue61a {ECO:0000313|EMBL:AFR29923.1,
RC   ECO:0000313|Proteomes:UP000003736};
RX   PubMed=23039946; DOI=10.1186/1471-2164-13-534;
RA   Niewerth H., Schuldes J., Parschat K., Kiefer P., Vorholt J.A.,
RA   Daniel R., Fetzner S.;
RT   "Complete genome sequence and metabolic potential of the quinaldine-
RT   degrading bacterium Arthrobacter sp. Rue61a.";
RL   BMC Genomics 13:534-534(2012).
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; CP003203; AFR29923.1; -; Genomic_DNA.
DR   RefSeq; WP_014922363.1; NC_018531.1.
DR   ProteinModelPortal; J7LTW9; -.
DR   EnsemblBacteria; AFR29923; AFR29923; ARUE_c30380.
DR   KEGG; arr:ARUE_c30380; -.
DR   PATRIC; fig|1118963.3.peg.3132; -.
DR   KO; K01775; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000003736; 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; -; 2.
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:UP000003736};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AFR29923.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      264    395       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   417 AA;  43486 MW;  63135B9C1BA1020A CRC64;
     MTYEAAADIG IGSKASIAKS AVLERSAVID LDAVRHNVRQ FVGIASPAAV MAVVKADAYG
     HGAVQVARAA LDAGAAWLGV AHISEALALR AAGVEAPLLA WLHTRESNFQ AAVAAGIDVG
     ISGWELEAVV AAAREQERPA RVHLKVDTGL GRNGCTIADW DQLLGQAMEY QDQGLLRVVG
     VFSHLAVADE PERPETDEQL AVFREALAMA EDAGVDTEVR HIANTPAALS RPDSHFDLVR
     VGLGIYGLSP FDGATSAELG LHPAMTVRTL LSNCKKVPEG QGVSYGLNYR TREESTLGLV
     PMGYADGVPR IATGGPVRVN GINYPVVGRI AMDQMVIDLG PLSPEAAAGL KGAEAVMFGN
     GADGGPTADD WAAAAGTNNY EIVTRISPRV PRSYVNEMPA QPHAPAVVSG QAETAAL
//
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