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Database: UniProt/TrEMBL
Entry: D9QEI2_CORP2
LinkDB: D9QEI2_CORP2
Original site: D9QEI2_CORP2 
ID   D9QEI2_CORP2            Unreviewed;       370 AA.
AC   D9QEI2;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-SEP-2017, entry version 54.
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:ADL09905.1};
GN   OrderedLocusNames=CpC231_0415 {ECO:0000313|EMBL:ADL09905.1};
OS   Corynebacterium pseudotuberculosis (strain C231).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=681645 {ECO:0000313|EMBL:ADL09905.1, ECO:0000313|Proteomes:UP000000276};
RN   [1] {ECO:0000313|EMBL:ADL09905.1, ECO:0000313|Proteomes:UP000000276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C231 {ECO:0000313|EMBL:ADL09905.1,
RC   ECO:0000313|Proteomes:UP000000276};
RX   PubMed=21037006; DOI=10.1128/JB.01211-10;
RG   Consortium: Rede Paraense de Genomica e Proteomica (RPGP);
RA   Silva A., Schneider M.P., Cerdeira L., Barbosa M.S., Ramos R.T.,
RA   Carneiro A.R., Santos R., Lima M., D'Afonseca V., Almeida S.S.,
RA   Santos A.R., Soares S.C., Pinto A.C., Ali A., Dorella F.A., Rocha F.,
RA   de Abreu V.A., Trost E., Tauch A., Shpigel N., Miyoshi A., Azevedo V.;
RT   "Complete genome sequence of Corynebacterium pseudotuberculosis I19, a
RT   strain isolated from a cow in Israel with bovine mastitis.";
RL   J. Bacteriol. 193:323-324(2011).
RN   [2] {ECO:0000313|EMBL:ADL09905.1, ECO:0000313|Proteomes:UP000000276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C231 {ECO:0000313|EMBL:ADL09905.1,
RC   ECO:0000313|Proteomes:UP000000276};
RX   PubMed=21533164; DOI=10.1371/journal.pone.0018551;
RA   Ruiz J.C., D'Afonseca V., Silva A., Ali A., Pinto A.C., Santos A.R.,
RA   Rocha A.A., Lopes D.O., Dorella F.A., Pacheco L.G., Costa M.P.,
RA   Turk M.Z., Seyffert N., Moraes P.M., Soares S.C., Almeida S.S.,
RA   Castro T.L., Abreu V.A., Trost E., Baumbach J., Tauch A.,
RA   Schneider M.P., McCulloch J., Cerdeira L.T., Ramos R.T., Zerlotini A.,
RA   Dominitini A., Resende D.M., Coser E.M., Oliveira L.M., Pedrosa A.L.,
RA   Vieira C.U., Guimaraes C.T., Bartholomeu D.C., Oliveira D.M.,
RA   Santos F.R., Rabelo E.M., Lobo F.P., Franco G.R., Costa A.F.,
RA   Castro I.M., Dias S.R., Ferro J.A., Ortega J.M., Paiva L.V.,
RA   Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P., Falcao P.R.,
RA   Grynberg P., Teixeira S.M., Brommonschenkel S., Oliveira S.C.,
RA   Meyer R., Moore R.J., Miyoshi A., Oliveira G.C., Azevedo V.;
RT   "Evidence for reductive genome evolution and lateral acquisition of
RT   virulence functions in two Corynebacterium pseudotuberculosis
RT   strains.";
RL   PLoS ONE 6:E18551-E18551(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}.
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; CP001829; ADL09905.1; -; Genomic_DNA.
DR   RefSeq; WP_014401000.1; NC_017301.1.
DR   ProteinModelPortal; D9QEI2; -.
DR   EnsemblBacteria; ADL09905; ADL09905; CpC231_0415.
DR   GeneID; 12298152; -.
DR   KEGG; cpq:CpC231_0415; -.
DR   PATRIC; fig|681645.3.peg.433; -.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000276; 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:UP000000276};
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:UP000000276}.
FT   DOMAIN      241    367       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     36     36       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    262    262       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     135    135       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     310    310       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      36     36       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   370 AA;  39912 MW;  8F524C63B7CA7940 CRC64;
     MNLLEARIDL AAIAHNTRLI KDKAAAQGAQ LMCVVKADGY NHGAVEVATV MEENGADQFG
     VATIGEGLAL REGGIESSIL SWIWSPEQDL GAAITAEIDL AAISLEHVKA LVRASESYGK
     KPVRVTVKVD TGLHRSGVDK QDWRESFCML RDAENIQVTG VFSHFSSADE SDSTETEQQE
     RAFLNAIELG RSLGLELPVN HIANSPATLN RPDLYFDMVR PGLALYGHEP IPGESHGLRE
     AMSWVGRVTV VKPIARGEGT SYGLTWRAEQ DGYLCVVPVG YADGLPRSAQ GHLEITIGGR
     RYPQVGRVCM DQIVVALGEN PYGVAQGDEA VILGPTGMTA TELATAMGTI NYELVCRPCG
     RTVRVFEHSD
//
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