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Database: UniProt/TrEMBL
Entry: A0A0A1FJY6_9BURK
LinkDB: A0A0A1FJY6_9BURK
Original site: A0A0A1FJY6_9BURK 
ID   A0A0A1FJY6_9BURK        Unreviewed;       368 AA.
AC   A0A0A1FJY6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   07-JUN-2017, entry version 20.
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=LT85_4821 {ECO:0000313|EMBL:AIY43979.1};
OS   Collimonas arenae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=279058 {ECO:0000313|EMBL:AIY43979.1, ECO:0000313|Proteomes:UP000030302};
RN   [1] {ECO:0000313|EMBL:AIY43979.1, ECO:0000313|Proteomes:UP000030302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cal35 {ECO:0000313|EMBL:AIY43979.1,
RC   ECO:0000313|Proteomes:UP000030302};
RA   Uroz S., Tech J.J., Sawaya N.A., Frey-Klett P., Leveau J.H.J.;
RT   "Structure and function of bacterial communities in ageing soils:
RT   insights from the Mendocino ecological staircase.";
RL   Soil Biol. Biochem. 69:265-274(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; CP009962; AIY43979.1; -; Genomic_DNA.
DR   RefSeq; WP_038494036.1; NZ_CP009962.1.
DR   EnsemblBacteria; AIY43979; AIY43979; LT85_4821.
DR   KEGG; care:LT85_4821; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000030302; 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:UP000030302};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AIY43979.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
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     139    139       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   368 AA;  39369 MW;  BF04154E6078FC2A CRC64;
     MNPQALHAGA ILRVDLNAVR SNYRFLRQRA GNALCAAAVK ANAYGLGADK VGPALAAEGC
     RHFFVAHLDE GIALRPHLPA TADIFVLHGP PPGAERELIA HGLTPVLNSL QQIEAWHALA
     QSLQRPLPAI FQVDTGMSRM GLPAAEAEAW LANPAFMESI PPLFLMSHLA CAEHQSHPMN
     ASQLARFKTW RQRLPQVAAS LANSSGIFLG SDFQFDLVRP GAALYGIAPV AGAENPLQAV
     VALHGRIIQS RTIQRGDHVG YGISYSATEE RQIATVGVGY ADGWLRSMSN RGIAFIDGRP
     APMVGTVSMD SITIDVTGIA AERVQAGALV ELIGPHRPVD EVAKLAGSIG YEILTDLGRR
     YHREYLGA
//
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