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Database: UniProt/TrEMBL
Entry: F2J1N5_POLGS
LinkDB: F2J1N5_POLGS
Original site: F2J1N5_POLGS 
ID   F2J1N5_POLGS            Unreviewed;       415 AA.
AC   F2J1N5;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   07-JUN-2017, entry version 49.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   OrderedLocusNames=SL003B_2411 {ECO:0000313|EMBL:ADZ70836.1};
OS   Polymorphum gilvum (strain LMG 25793 / CGMCC 1.9160 / SL003B-26A1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Polymorphum.
OX   NCBI_TaxID=991905 {ECO:0000313|EMBL:ADZ70836.1, ECO:0000313|Proteomes:UP000008130};
RN   [1] {ECO:0000313|EMBL:ADZ70836.1, ECO:0000313|Proteomes:UP000008130}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 25793 / CGMCC 1.9160 / SL003B-26A1
RC   {ECO:0000313|Proteomes:UP000008130};
RX   PubMed=21478361; DOI=10.1128/JB.00333-11;
RA   Li S.G., Tang Y.Q., Nie Y., Cai M., Wu X.L.;
RT   "Complete genome sequence of Polymorphum gilvum SL003B-26A1T, a crude
RT   oil-degrading bacterium from oil-polluted saline soil.";
RL   J. Bacteriol. 193:2894-2895(2011).
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; CP002568; ADZ70836.1; -; Genomic_DNA.
DR   ProteinModelPortal; F2J1N5; -.
DR   STRING; 991905.SL003B_2411; -.
DR   EnsemblBacteria; ADZ70836; ADZ70836; SL003B_2411.
DR   KEGG; pgv:SL003B_2411; -.
DR   PATRIC; fig|991905.3.peg.2471; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000008130; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
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:UP000008130};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008130}.
FT   DOMAIN      277    408       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     78     78       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    298    298       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     176    176       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     351    351       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      78     78       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   415 AA;  44238 MW;  E45EA3AD034CDE30 CRC64;
     MSRPQRLRIG YDWICLATAR DSPRFRTNAG AWVLPMSSVS PEALAGGVLT VDTAAIADNW
     RALAGQLGPG ARCAATVKAD AYGCGIPATV RALAASGCDT FFVALPAEGI AVREAAPGAT
     IYVLDGLFPG TAPAYAEARL RPVLGSLPEL EEWALFCRSR KVRLEAAVHV DTGMNRLGLT
     EQEAERLAGD RDLLDSFALA LVISHLACGA EPGHPLNRQQ LERFRTLSGH FPDAVRSLAN
     SAGIFLGADY HFDLVRPGIA LYGGKALDSF DNPMRPVARV EARILQLRTV RAGEGVGYGL
     AQTVRRDTRL AVVAAGYADG LLRRAGGSDD RPGGHGWIVG HRVPVFGRIS MDMQALDVTD
     VPAALLRRGA MVELIGPHVA ASELAAVADT IDYEYLTALG RRFHRRYAPL AEVAG
//
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