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Database: UniProt/TrEMBL
Entry: D5BRJ2_PUNMI
LinkDB: D5BRJ2_PUNMI
Original site: D5BRJ2_PUNMI 
ID   D5BRJ2_PUNMI            Unreviewed;       383 AA.
AC   D5BRJ2;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-SEP-2017, entry version 59.
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=SAR116_0646 {ECO:0000313|EMBL:ADE38889.1};
OS   Puniceispirillum marinum (strain IMCC1322).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; SAR116 cluster;
OC   Candidatus Puniceispirillum.
OX   NCBI_TaxID=488538 {ECO:0000313|EMBL:ADE38889.1, ECO:0000313|Proteomes:UP000007460};
RN   [1] {ECO:0000313|EMBL:ADE38889.1, ECO:0000313|Proteomes:UP000007460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC1322 {ECO:0000313|EMBL:ADE38889.1,
RC   ECO:0000313|Proteomes:UP000007460};
RX   PubMed=20382761; DOI=10.1128/JB.00347-10;
RA   Oh H.M., Kwon K.K., Kang I., Kang S.G., Lee J.H., Kim S.J., Cho J.C.;
RT   "Complete genome sequence of "Candidatus Puniceispirillum marinum"
RT   IMCC1322, a representative of the SAR116 clade in the
RT   Alphaproteobacteria.";
RL   J. Bacteriol. 192:3240-3241(2010).
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}.
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}.
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DR   EMBL; CP001751; ADE38889.1; -; Genomic_DNA.
DR   RefSeq; WP_013045518.1; NC_014010.1.
DR   ProteinModelPortal; D5BRJ2; -.
DR   STRING; 488538.SAR116_0646; -.
DR   EnsemblBacteria; ADE38889; ADE38889; SAR116_0646.
DR   KEGG; apb:SAR116_0646; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031445; -.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000007460; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007460};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:ADE38889.1};
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:UP000007460}.
FT   DOMAIN      257    383       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     48     48       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    278    278       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     151    151       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     326    326       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      48     48       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   383 AA;  42040 MW;  C94F1188C70B9228 CRC64;
     MSTGDENVLA AFGAADNRID IDLGAIAHNW LYLDSLSPKS TITAAMVKAN GYGLGANHVG
     AALYKAGCRQ FFVANLDEAV SFRTYLDNIS ISDAQIMVLH GCHRGQEHDM RAYRLTPVLN
     DLEQVSRWRL YAQNANETYP AMLHLDTGMT RLGFDPDQTD WLIENKQALN GLEITYIMSH
     LISGEISDDP ANTAQKTRFD EYRSFFGGIK ASLANSGGVF LGNEFHYQMT RPGIAIYGVH
     PCGKDQAITD SNGLKSCITW HGRIIQVRTA PEGATVGYGG THRLSRPSRI ATVGVGYADG
     YQRNLSNKAF VNILGHRAPV IGRISMDSIT IDVTDIPPNI MLKAETAALL SDLYSIEDMA
     NDASTIPYEI LTGISRRAIR RYI
//
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