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Database: UniProt/TrEMBL
Entry: X5DRG2_9CORY
LinkDB: X5DRG2_9CORY
Original site: X5DRG2_9CORY 
ID   X5DRG2_9CORY            Unreviewed;       603 AA.
AC   X5DRG2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-SEP-2017, entry version 27.
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:AHW63252.1};
GN   ORFNames=CGLY_04020 {ECO:0000313|EMBL:AHW63252.1};
OS   Corynebacterium glyciniphilum AJ 3170.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1404245 {ECO:0000313|EMBL:AHW63252.1, ECO:0000313|Proteomes:UP000023703};
RN   [1] {ECO:0000313|EMBL:AHW63252.1, ECO:0000313|Proteomes:UP000023703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AJ 3170 {ECO:0000313|EMBL:AHW63252.1};
RX   PubMed=25323597; DOI=10.1099/ijs.0.065102-0;
RA   Al-Dilaimi A., Bednarz H., Lomker A., Niehaus K., Kalinowski J.,
RA   Ruckert C.;
RT   "Revisiting Corynebacterium glyciniphilum (ex Kubota et al., 1972) sp.
RT   nov., nom. rev., isolated from putrefied banana.";
RL   Int. J. Syst. Evol. Microbiol. 65:177-182(2015).
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; CP006842; AHW63252.1; -; Genomic_DNA.
DR   EnsemblBacteria; AHW63252; AHW63252; CGLY_04020.
DR   KEGG; cgy:CGLY_04020; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000023703; 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   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR003442; T6A_TsaE.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   Pfam; PF02367; TsaE; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   TIGRFAMs; TIGR00150; T6A_YjeE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000023703};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AHW63252.1};
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:UP000023703}.
FT   DOMAIN      273    404       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    294    294       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     156    156       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     342    342       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   603 AA;  62753 MW;  F28DCF35BE4A7227 CRC64;
     MSERSGRDLC DHHDPRDHAL AELVVDLGAI DHNVRTLVRI AAPAGVMAIV KADGYNHGMV
     DVARTALDAG AVALGVATLG EALALRDAGV TAPVTAWMWL PDPDQEDIAA ACTAGVTLGV
     PSVEHLHAAV AASRSAVAGG SSPLTVGLMA DTGLSRSGIE AARWDEAVSL AVAAVRDGVL
     TVSGVLSHLA SADDPASPVT DLQARRFVAA VETCRAMGLD VPVNHIANTP ATLSRPDLRH
     EMVRPGVSVY GVYAVDPTVI PVGESGPVRL REAMTVRARV VTTRVVPAGE GVSYGHLWRA
     ERDTRTAVVA IGYADGVPRN MSGRFGVTVN GVWFPQIGRV CMDQIVIDLG AAGEDGPGAS
     VRPGDWAVIF GTGGRSVEEI ATAAGTIAYE VLTLPRGRVR RRVLPTTPAA DEGPFTGVFD
     AASGTVEVSS AESMRALGRE LGRQLRAGDV VVLTGALGAG KTTVTQGIAT GLGVKGRVQS
     PTFTIIREHR PGTDGTGRPG MLHMDAYRLL GEGAHGSGPD SGPTRGAVLD ALESLDIDAD
     LEDRVLVAEW GRGVVESLAP ARWIDIEIDR SGGDGSDGDS DGDSDVGYED ESPRQFHWRW
     SQG
//
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