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Database: UniProt/TrEMBL
Entry: A0A127QC09_9BURK
LinkDB: A0A127QC09_9BURK
Original site: A0A127QC09_9BURK 
ID   A0A127QC09_9BURK        Unreviewed;       368 AA.
AC   A0A127QC09;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-SEP-2017, entry version 11.
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:AMP07554.1};
GN   ORFNames=CPter91_5268 {ECO:0000313|EMBL:AMP07554.1};
OS   Collimonas pratensis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=279113 {ECO:0000313|EMBL:AMP07554.1, ECO:0000313|Proteomes:UP000074561};
RN   [1] {ECO:0000313|EMBL:AMP07554.1, ECO:0000313|Proteomes:UP000074561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter91 {ECO:0000313|EMBL:AMP07554.1,
RC   ECO:0000313|Proteomes:UP000074561};
RA   Song C., Schmidt R., de Jager V., Krzyzanowska D., Jongedijk E.,
RA   Cankar K., Beekwilder J., van Veen A., de Boer W., van Veen J.A.,
RA   Garbeva P.;
RT   "Exploring the genomic traits of fungus-feeding bacterial genus
RT   Collimonas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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; CP013234; AMP07554.1; -; Genomic_DNA.
DR   RefSeq; WP_061945219.1; NZ_CP013234.1.
DR   EnsemblBacteria; AMP07554; AMP07554; CPter91_5268.
DR   KEGG; cpra:CPter91_5268; -.
DR   PATRIC; fig|279113.9.peg.5221; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000074561; 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:UP000074561};
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}.
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;  38980 MW;  BC6A1C2F4C3839A9 CRC64;
     MNPQAAHAGA ILTVNLDAIR GNYRLLRQQA GKAACAAAVK ANAYGLGADK VGPALAAEGC
     RHFFVAHLDE GIALRPHLPA TADIFVLHGA PPGTERELIA HGLTPVLNSL QQIAAWHALA
     QTLQRPLPAI FQVDTGMSRM GLPAAEAEAW LANPAFMESI PPLFLMSHLA CAEHQGHPMN
     ASQLARFLAW RQRLPQVAAS LANSSGIFLG PDYQFDLVRP GAALFGIAPV AGAANPLQPV
     VALHGRIIQS RTIQRGDHVG YGISYSASEE RQIATVGVGY ADGWLRSMSN RGIAFIDGQP
     APMVGTVSMD SITIDVTGIA AERVQAGATV ELIGPQRPLD DVARLAGSIG YEILTDLGRR
     YHREYIGG
//
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