GenomeNet

Database: UniProt/TrEMBL
Entry: A0A172QRI0_9CORY
LinkDB: A0A172QRI0_9CORY
Original site: A0A172QRI0_9CORY 
ID   A0A172QRI0_9CORY        Unreviewed;       361 AA.
AC   A0A172QRI0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-SEP-2017, entry version 10.
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=ccrud_03000 {ECO:0000313|EMBL:ANE03281.1};
OS   Corynebacterium crudilactis.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1652495 {ECO:0000313|EMBL:ANE03281.1, ECO:0000313|Proteomes:UP000076929};
RN   [1] {ECO:0000313|EMBL:ANE03281.1, ECO:0000313|Proteomes:UP000076929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JZ16 {ECO:0000313|EMBL:ANE03281.1,
RC   ECO:0000313|Proteomes:UP000076929};
RA   Christian R., Zimmermann J., Lipski A., Kalinowski J.;
RT   "Complete genome sequence of Corynebacterium crudilactis, a new
RT   Corynebacterium species isolated from raw cow's milk.";
RL   Submitted (MAY-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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP015622; ANE03281.1; -; Genomic_DNA.
DR   RefSeq; WP_066564663.1; NZ_CP015622.1.
DR   EnsemblBacteria; ANE03281; ANE03281; ccrud_03000.
DR   KEGG; ccjz:ccrud_03000; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000076929; 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:UP000076929};
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      235    361       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    256    256       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     129    129       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     304    304       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      34     34       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   361 AA;  39014 MW;  DF8708E655671F55 CRC64;
     MNLLTTKIDL NAIAHNTRVL KQMAGSAKLM AVVKANAYNH GIEEVAPVIA AHGADAFGVA
     TLAEAHQLRD LGIEQEVLCW IWTPEQDFRA ALDRGIDLGV VSPKHARAVI ATEAEHIRVT
     VKVETGLHRS GVDEDEWAEV FSALAAAPHV EVTGLFTHLS CADDPADPET DRQVAAFRRA
     LALARELGLE CPVNHVCNSP AFLTRADLHM EMVRPGLAFY GLEPVDGLDH GLQPAMSWTA
     KVSVVKQIEA GQGTSYGLTW RAEDSGYVAV VPAGYADGLP RFAQEKFSVT INGVDYPQVG
     RICMDQFVIF LGDNPHGVEA GAEAVIFGEN GHGATDFAQR LGTINYEVVC RPTGRTVREY
     I
//
DBGET integrated database retrieval system