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Database: UniProt/TrEMBL
Entry: A0A0H4W1N3_9BORD
LinkDB: A0A0H4W1N3_9BORD
Original site: A0A0H4W1N3_9BORD 
ID   A0A0H4W1N3_9BORD        Unreviewed;       376 AA.
AC   A0A0H4W1N3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   12-SEP-2018, entry version 19.
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=dadX {ECO:0000313|EMBL:AKQ54684.1};
GN   ORFNames=ACR54_01347 {ECO:0000313|EMBL:AKQ54684.1};
OS   Bordetella hinzii.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=103855 {ECO:0000313|EMBL:AKQ54684.1, ECO:0000313|Proteomes:UP000036382};
RN   [1] {ECO:0000313|Proteomes:UP000036382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F582 {ECO:0000313|Proteomes:UP000036382};
RA   Weigand M.R., Changayil S., Kulasekarapandian Y., Batra D.,
RA   Williams M.M., Tondella M.L.;
RT   "Complete Genome Sequences of Two Bordetella hinzii Isolated from
RT   Humans.";
RL   Submitted (JUL-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|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; CP012076; AKQ54684.1; -; Genomic_DNA.
DR   RefSeq; WP_029579342.1; NZ_LT906461.1.
DR   EnsemblBacteria; AKQ54684; AKQ54684; ACR54_01347.
DR   GeneID; 29513161; -.
DR   KEGG; bhz:ACR54_01347; -.
DR   PATRIC; fig|103855.15.peg.1336; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000036382; 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:UP000036382};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AKQ54684.1};
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:UP000036382}.
FT   DOMAIN      250    375       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     44     44       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    271    271       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     319    319       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      44     44       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   376 AA;  39911 MW;  C3A85F9A791B8362 CRC64;
     MPRPISALIS PSALRHNLSV VRQRLDRQAE VEGGVSPSIW AVIKANAYGH GIERAVGAFS
     EAQGLAMLDL EEAVRCREAG WGGPIMLLEG FFQPRDLDLL DRYHLSTAIH CQEQLDMLAH
     ARPAHRINAM LKLNSGMNRL GFAPDAYARA FEAARALQGR GVLGTVGKMT HFATADGPQG
     PQWQWEVFEA ATQGLPGPVS VCNSAGTLRY PRLAIGRAGQ DTHWVRPGIC LYGASPFDDQ
     SAAELGLRPA MTLRSELIGV QHLQPGQTVG YGATFTAPRA MRIGVVACGY ADGYPRHCGT
     GTPITVAGVP TRLLGRVSMD MLAVDLEPVA AAGVGSPVVL WGEGGPGVDE VAAAAGTIGY
     ELLTALAQRV PVTEIR
//
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