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Database: UniProt/TrEMBL
Entry: H2JT65_STRHJ
LinkDB: H2JT65_STRHJ
Original site: H2JT65_STRHJ 
ID   H2JT65_STRHJ            Unreviewed;       381 AA.
AC   H2JT65;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   28-FEB-2018, entry version 48.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   OrderedLocusNames=SHJG_5842 {ECO:0000313|EMBL:AEY91109.1};
OS   Streptomyces hygroscopicus subsp. jinggangensis (strain 5008).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1133850 {ECO:0000313|EMBL:AEY91109.1, ECO:0000313|Proteomes:UP000007170};
RN   [1] {ECO:0000313|Proteomes:UP000007170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5008 {ECO:0000313|Proteomes:UP000007170};
RA   Wu H., Bai L.;
RT   "Genomic analysis of Streptomyces hygroscopicus subsp. jinggangensis
RT   5008.";
RL   Submitted (JAN-2012) 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}.
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DR   EMBL; CP003275; AEY91109.1; -; Genomic_DNA.
DR   ProteinModelPortal; H2JT65; -.
DR   STRING; 1133850.SHJG_5842; -.
DR   EnsemblBacteria; AEY91109; AEY91109; SHJG_5842.
DR   KEGG; shy:SHJG_5842; -.
DR   PATRIC; fig|1133850.20.peg.6421; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; POG091H022F; -.
DR   BioCyc; SHYG1133850:GLLU-5895-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000007170; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007170};
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:UP000007170}.
FT   DOMAIN      250    377       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   COILED        7     27       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE     38     38       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     136    136       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      38     38       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   381 AA;  39800 MW;  39F55575B6DA4D07 CRC64;
     MPTAALRARA EIDLGALRAN VRALRARAEG AALMAVVKSD GYGHGAVPCA RAALAAGASW
     LGTATAEEAL ALRAAGLPGR ILCWLWVPGG PWRQAIEADI DVSLSGMWAL REVVDAARAA
     GRTARVHLKA DTGLGRNGCQ PGEDWAELVG AAVRAEAEGL VRVTGVWSHF ACADEPGHPS
     VAAQLTRFRE MLAYAEEQGV RPEVRHIANS PATLTLPEAH FDLVRTGIAL YGVSPSPELG
     TPADFGLRPV MTLSASLALV KRTPAGHGVS YGHHYVTPGE TTLGLVPVGY ADGIPRHASG
     TGPVLVGGKW RTIAGRVAMD QFVVDLGGDE PPVGSEAVLF GPGDRGEPTA EDWAQACGTI
     AYEIVTRIGT RVPRVYVNAS M
//
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