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Database: UniProt/TrEMBL
Entry: A0A193GCP8_9BORD
LinkDB: A0A193GCP8_9BORD
Original site: A0A193GCP8_9BORD 
ID   A0A193GCP8_9BORD        Unreviewed;       382 AA.
AC   A0A193GCP8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   25-OCT-2017, entry version 13.
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=BAU07_09055 {ECO:0000313|EMBL:ANN77231.1};
OS   Bordetella flabilis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=463014 {ECO:0000313|EMBL:ANN77231.1, ECO:0000313|Proteomes:UP000091926};
RN   [1] {ECO:0000313|EMBL:ANN77231.1, ECO:0000313|Proteomes:UP000091926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU10664 {ECO:0000313|EMBL:ANN77231.1,
RC   ECO:0000313|Proteomes:UP000091926};
RA   LiPuma J.J., Spilker T.;
RT   "Complete genome sequences of Bordetella bronchialis and Bordetella
RT   flabilis.";
RL   Submitted (JUN-2016) 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}.
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; CP016172; ANN77231.1; -; Genomic_DNA.
DR   RefSeq; WP_066656343.1; NZ_CP016172.1.
DR   EnsemblBacteria; ANN77231; ANN77231; BAU07_09055.
DR   KEGG; bfz:BAU07_09055; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000091926; 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:UP000091926};
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:UP000091926}.
FT   DOMAIN      256    381       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     51     51       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    277    277       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     146    146       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     325    325       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      51     51       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   382 AA;  40408 MW;  BA89E7A8E8072253 CRC64;
     MPRPISVTIS VSALAHNLGV VRQHLDQATA AGAARSAGTP RVPPSIWAVI KAHGYGHGIE
     QAMQGFAQAD GLAMLDLAEA AHCRESGWGK PLLLLEGYFE PDDLHVVDRH RLTTVVHCQP
     QLDMLARFRP QHPLNIFLKL NTGMNRLGFE PGAYRQAYRH AQELQARGVV GTLGRMTHFA
     NADGPQGIAA QHDVFRRVAG DLPGPASVCN SAATLRYPEI AVADSPAASW VRPGICLYGA
     SPFFDTDAAS FGLRPAMSLR SRIIAIQALQ PGDTVGYGSL FTAQAPTRVG VVACGYADGY
     PRHAGTGTPI VVEGVRTRVL GRVSMDMLAV DLTPVPDASI GAPVSLWGAD GPSVDEVAQA
     AGTIGYELLC ALAPRVPVRT TP
//
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