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Database: UniProt/TrEMBL
Entry: V6EZS6_9PROT
LinkDB: V6EZS6_9PROT
Original site: V6EZS6_9PROT 
ID   V6EZS6_9PROT            Unreviewed;       370 AA.
AC   V6EZS6;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-SEP-2017, entry version 29.
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:CDK98709.1};
GN   ORFNames=MGMSRv2__1494 {ECO:0000313|EMBL:CDK98709.1};
OS   Magnetospirillum gryphiswaldense MSR-1 v2.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=1430440 {ECO:0000313|EMBL:CDK98709.1, ECO:0000313|Proteomes:UP000018922};
RN   [1] {ECO:0000313|EMBL:CDK98709.1, ECO:0000313|Proteomes:UP000018922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSR-1 {ECO:0000313|EMBL:CDK98709.1};
RX   PubMed=24625872; DOI=10.1128/genomeA.00171-14;
RA   Wang X., Wang Q., Zhang W., Wang Y., Li L., Wen T., Zhang T.,
RA   Zhang Y., Xu J., Hu J., Li S., Liu L., Liu J., Jiang W., Tian J.,
RA   Li Y., Schuler D., Wang L., Li J.;
RT   "Complete Genome Sequence of Magnetospirillum gryphiswaldense MSR-1.";
RL   Genome Announc. 2:e00171-e00114(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; HG794546; CDK98709.1; -; Genomic_DNA.
DR   ProteinModelPortal; V6EZS6; -.
DR   EnsemblBacteria; CDK98709; CDK98709; MGMSRv2__1494.
DR   KEGG; mgy:MGMSRv2__1494; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000018922; 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:UP000018922};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:CDK98709.1};
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:UP000018922}.
FT   DOMAIN      240    366       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     40     40       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    261    261       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     138    138       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     309    309       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      40     40       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   370 AA;  38938 MW;  46CEEA1FE07F3E14 CRC64;
     MMTAHDRATG ILSIDLDAIA DNWRTLAAHA PNAEAAGVVK ADGYGLGAAP VARALRKAGC
     TTFFVATIDE GISLRPHVND ARILVLGGVL PGTGADFIGH QLIPVLNSPE QIGLWSGFAA
     AGGRPLPAAI HMDSGMNRLG LDETAVELLA ADNRRLDGIQ PVLVMSHMAC ADERDHAMNR
     QQLDRFTVLA DRLGVSAPRS LAASSTIFLG ADYHFDLIRP GAGLYGINPM PDSPNPLRQT
     VRLHGKILQV RDVDTPQTVG YGASHRFKSK GRVATIACGY ADGLFRSLGN RGFGVIGGVK
     VPVVGRISMD LITLDVSAVA PAHVHAGALV ELIGPDHDVD ALAAEAGTIG YEILTSLGRR
     YLRDYSGGNT
//
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