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Database: UniProt/TrEMBL
Entry: F8JZB6_STREN
LinkDB: F8JZB6_STREN
Original site: F8JZB6_STREN 
ID   F8JZB6_STREN            Unreviewed;       391 AA.
AC   F8JZB6; G8X007;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   28-FEB-2018, entry version 57.
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=SCATT_36270 {ECO:0000313|EMBL:AEW95998.1};
OS   Streptomyces cattleya (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC
OS   14057 / NRRL 8057).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1003195 {ECO:0000313|EMBL:AEW95998.1, ECO:0000313|Proteomes:UP000007842};
RN   [1] {ECO:0000313|Proteomes:UP000007842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057
RC   {ECO:0000313|Proteomes:UP000007842};
RA   Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.;
RT   "Complete genome sequence of Streptomyces cattleya strain DSM 46488.";
RL   Submitted (DEC-2011) 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; CP003219; AEW95998.1; -; Genomic_DNA.
DR   RefSeq; WP_014144354.1; NC_017586.1.
DR   ProteinModelPortal; F8JZB6; -.
DR   STRING; 1003195.SCAT_3633; -.
DR   EnsemblBacteria; AEW95998; AEW95998; SCATT_36270.
DR   KEGG; sct:SCAT_3633; -.
DR   KEGG; scy:SCATT_36270; -.
DR   PATRIC; fig|1003195.11.peg.5099; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000007842; 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:UP000007842};
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:UP000007842}.
FT   DOMAIN      255    382       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    276    276       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     142    142       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     324    324       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   391 AA;  40711 MW;  FA38CE681E30D01D CRC64;
     MNEDEAPGTT ARTWAEIDLA ALRANVGALR SRLTGGAALM AVVKADAYGH GMVPCARAAR
     AAGAEWLGTA TPQEALALRA AGVDGRVLCW LWTPGGPWRE AIEADVDVTV SGMWALREVT
     AAARAAGRPA RVQLKADTGL GRNGCQPHDW PELVAAARAA ERDGLLRVTG VWSHFACADE
     PGHPSIAAQL TAFRQALATA EAAGLDPEVR HIANSPATLT LPESHFDLVR TGVSMYGISP
     VPQLAGPAEY GLRPVMTLLA NVASVKRVPG GHGVSYGHLY TTPGQTTLAL IPAGYADGIP
     RHASGTGPVL VAGKWRTVAG RVAMDQFVVD LGGDTARTGE RAVLFGPGDR GEPTAEDWAR
     AAGTIAYEIV TRIGPRVPRV HLGADDGPVG R
//
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