GenomeNet

Database: UniProt/TrEMBL
Entry: A0A0S2JNP0_ALCFA
LinkDB: A0A0S2JNP0_ALCFA
Original site: A0A0S2JNP0_ALCFA 
ID   A0A0S2JNP0_ALCFA        Unreviewed;       376 AA.
AC   A0A0S2JNP0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   28-FEB-2018, entry version 15.
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=UZ73_05020 {ECO:0000313|EMBL:ALO37681.1};
OS   Alcaligenes faecalis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Alcaligenes.
OX   NCBI_TaxID=511 {ECO:0000313|EMBL:ALO37681.1, ECO:0000313|Proteomes:UP000056606};
RN   [1] {ECO:0000313|EMBL:ALO37681.1, ECO:0000313|Proteomes:UP000056606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZD02 {ECO:0000313|EMBL:ALO37681.1,
RC   ECO:0000313|Proteomes:UP000056606};
RA   Ju S., Zheng J., Sun M.;
RT   "The complete genome sequence of Alcaligenes faecalis ZD02, a novel
RT   potential bionematocide.";
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP013119; ALO37681.1; -; Genomic_DNA.
DR   RefSeq; WP_045931122.1; NZ_MSZR01000037.1.
DR   EnsemblBacteria; ALO37681; ALO37681; UZ73_05020.
DR   GeneID; 29369990; -.
DR   KEGG; afa:UZ73_05020; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000056606; 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; -; 2.
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:UP000056606};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:ALO37681.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
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;  39967 MW;  70AE920CFFFEBE70 CRC64;
     MPRPISATIH IASLRHNLDM VIQSLNNATA PSGVKRPHIW AVMKANAYGH DIENAVRAFS
     AAEGMAMLDL KEAIRCRAAG WTGPIMLLEG FFQPEDLDVL AEFGLTTVIH CHEQLKMLEQ
     WKGGVALNAM VKLNSGMNRL GFSVDDYPAA FERAQRLQKA GKLGTVGRMT HFARADDNID
     ATLEQIRCFD RITDGLPGPV SVCNSAATLS PDLGAYMPSG PDHWVRPGIC LYGSSPFADI
     SADDFGLQPG MTLAAELISV RGVKQGEGIG YGHTYIAEQA MRVGVVACGY ADGYPRHAGT
     GTPITVNGVR TRLLGRVSMD MLAVDLTPVP AAGVGSQAVL FGQGGPSVDE VAAAAGTLGY
     ELICAVAPRV PRIIQD
//
DBGET integrated database retrieval system