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Database: UniProt/TrEMBL
Entry: M1NJM4_9CORY
LinkDB: M1NJM4_9CORY
Original site: M1NJM4_9CORY 
ID   M1NJM4_9CORY            Unreviewed;       365 AA.
AC   M1NJM4;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-SEP-2017, entry version 33.
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=alr {ECO:0000313|EMBL:AGF71593.1};
GN   ORFNames=A605_02895 {ECO:0000313|EMBL:AGF71593.1};
OS   Corynebacterium halotolerans YIM 70093 = DSM 44683.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1121362 {ECO:0000313|EMBL:AGF71593.1, ECO:0000313|Proteomes:UP000011723};
RN   [1] {ECO:0000313|EMBL:AGF71593.1, ECO:0000313|Proteomes:UP000011723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 70093 {ECO:0000313|EMBL:AGF71593.1};
RX   PubMed=23408721;
RA   Ruckert C., Albersmeier A., Al-Dilaimi A., Niehaus K.,
RA   Szczepanowski R., Kalinowski J.;
RT   "Genome sequence of the halotolerant bacterium Corynebacterium
RT   halotolerans type strain YIM 70093(T) (= DSM 44683(T)).";
RL   Stand. Genomic Sci. 7:284-293(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; CP003697; AGF71593.1; -; Genomic_DNA.
DR   RefSeq; WP_015400014.1; NZ_JIAJ01000002.1.
DR   ProteinModelPortal; M1NJM4; -.
DR   EnsemblBacteria; AGF71593; AGF71593; A605_02895.
DR   KEGG; chn:A605_02895; -.
DR   PATRIC; fig|1121362.3.peg.581; -.
DR   KO; K01775; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000011723; 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:UP000011723};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AGF71593.1};
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:UP000011723}.
FT   DOMAIN      234    360       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    255    255       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     128    128       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     303    303       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      34     34       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   365 AA;  38774 MW;  5EB1E7E2D2F1DA87 CRC64;
     MDLLTARIDL DAIAHNTRLL KDLVGEARLM AVVKADGYGH GATEVAPVMA ANGADAFGVA
     TLAEAVELRE SGIETPILAW IWSPHQDVAE ALALNIELGV PSLEHARALV AAEVPARVCV
     KVDTGLHRSG VDEAEWDEVF TTLRDAAHLT VTGVFSHLSC ADEPDNPETD RQAERFRRAI
     ARARELGLEV PVNHLCNSPG ALTRADLHFG QVRVGVALYG QEPVPGLDHG LKPAMTWVGR
     VAVVKPIAPG EGTSYGLTWH AERAGRLAVI PCGYADGLPR MVQGHLEVGI GGKRYPQVGR
     VCMDQIVVDL GDNAADVRPG DEAVIFGAGG MSATELAEAT GTINYEIICL PTGRTVRTYT
     GGDQQ
//
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