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Database: UniProt/TrEMBL
Entry: A0A0M4DVQ0_9ACTN
LinkDB: A0A0M4DVQ0_9ACTN
Original site: A0A0M4DVQ0_9ACTN 
ID   A0A0M4DVQ0_9ACTN        Unreviewed;       517 AA.
AC   A0A0M4DVQ0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   23-MAY-2018, entry version 18.
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=ABE83_13600 {ECO:0000313|EMBL:ALC28017.1};
OS   Streptomyces sp. CFMR 7.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1649184 {ECO:0000313|EMBL:ALC28017.1, ECO:0000313|Proteomes:UP000061366};
RN   [1] {ECO:0000313|EMBL:ALC28017.1, ECO:0000313|Proteomes:UP000061366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFMR-7 {ECO:0000313|EMBL:ALC28017.1,
RC   ECO:0000313|Proteomes:UP000061366};
RA   Sudesh K.;
RT   "Complete genome sequence of Streptomyces sp strain CFMR 7, a natural
RT   rubber degrading Actinomycetes isolated from Penang, Malaysia.";
RL   Submitted (MAY-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}.
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DR   EMBL; CP011522; ALC28017.1; -; Genomic_DNA.
DR   RefSeq; WP_053559754.1; NZ_CP011522.1.
DR   EnsemblBacteria; ALC28017; ALC28017; ABE83_13600.
DR   KEGG; scz:ABE83_13600; -.
DR   PATRIC; fig|1649184.3.peg.2905; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000061366; 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:UP000061366};
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:UP000061366}.
FT   DOMAIN      250    377       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   COILED        8     35       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE     39     39       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     137    137       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      39     39       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   517 AA;  51782 MW;  CA4E3F9E013AFE28 CRC64;
     MNETASLRAR AEIDLAALRA NVRALRERAA GAQLMAVVKS DGYGHGAVPC ARAAREAGAT
     WLGTATPHEA LALRAAGLDG RIMCWLWTPG GPWREAIEAG IDVSVSALWS LREAVAGAAA
     AGRPARVQLK ADTGLGRAGC QPADWPALVA EARAAERTGA IRITGLWSHL ACADEPGHPS
     IAAQLSAFRD MVAYAEKEGV DPEVRHLANS PATLTLPETH FDLVRTGIAM YGISPAPELG
     TPAELGLRPV MTLAAAVALV KDVPAGHGVS YGHHYATADE TTLGLIPVGY ADGIPRHASG
     RGPVLVGGRV RTAAGRVAMD QFVVDLGGDR PEPGAEALLF GPGDQGEPSV EDWAVAADTI
     GYEIVTRIGT RVPRVYVNES AGAVDGSAGT VGRVSGAPEA GATSGRAATV HGTGSGAASG
     TAGTAGGTAA EHMNGAAAEY VNGAAASVAV NGTASAPANG TASATTAGTA GPVNGTAAGA
     GSEAVGHVNG VSTTAHEAAR TAPTTADPTR AEARRGE
//
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