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Database: UniProt/TrEMBL
Entry: A0A089QFB6_9RHIZ
LinkDB: A0A089QFB6_9RHIZ
Original site: A0A089QFB6_9RHIZ 
ID   A0A089QFB6_9RHIZ        Unreviewed;       390 AA.
AC   A0A089QFB6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-SEP-2017, entry version 18.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   ORFNames=MOC_5529 {ECO:0000313|EMBL:AIQ93284.1};
OS   Methylobacterium oryzae CBMB20.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=693986 {ECO:0000313|EMBL:AIQ93284.1, ECO:0000313|Proteomes:UP000029492};
RN   [1] {ECO:0000313|EMBL:AIQ93284.1, ECO:0000313|Proteomes:UP000029492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBMB20 {ECO:0000313|EMBL:AIQ93284.1};
RX   PubMed=25211235;
RA   Kwak M.J., Jeong H., Madhaiyan M., Lee Y., Sa T.M., Oh T.K., Kim J.F.;
RT   "Genome Information of Methylobacterium oryzae, a Plant-Probiotic
RT   Methylotroph in the Phyllosphere.";
RL   PLoS ONE 9:E106704-E106704(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; CP003811; AIQ93284.1; -; Genomic_DNA.
DR   EnsemblBacteria; AIQ93284; AIQ93284; MOC_5529.
DR   KEGG; mor:MOC_5529; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000029492; 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:UP000029492};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AIQ93284.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      263    388       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     63     63       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    284    284       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     162    162       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     331    331       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      63     63       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   390 AA;  39823 MW;  2EABDEB863B0D43C CRC64;
     MAAAHQGAAP GVAMSRIDRD HRPDAGPAGT AAALLTIDLG AIADNYRALA LQAGPAVCAA
     VVKADAYGLG ADRVAPVLAA AGCRHFFVAQ VGEGVALRAI LGPGPVIAVL NGASPGSEAA
     CAAHDLVPVL NDRSQRDGWQ GLARRLDRRL PAILQIDSGM ARFGFAPDEA CALLDAPDAL
     AGLDLQLVMS HLACAGEPDS PVNAAQRAVF EVVRRRLPAV PASLAASSGI FLGPDFRFDL
     VRPGAALYGI APQADAPNPM RPVIGLRARV MQTRSVPAGT PVGYGHAATV GRDSRLATVA
     IGYADGFFRS TAGGAAWFGG TRLPVVGRVS MDSLVLDVTD LAPGTIGPGA LVDIIGPERD
     VDAVAAAAGT IGYEVLTNLG HRFHRVYLGA
//
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