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Database: UniProt/TrEMBL
Entry: A0A1V0VB21_9ACTN
LinkDB: A0A1V0VB21_9ACTN
Original site: A0A1V0VB21_9ACTN 
ID   A0A1V0VB21_9ACTN        Unreviewed;       395 AA.
AC   A0A1V0VB21;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   25-APR-2018, entry version 11.
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=B7C62_22380 {ECO:0000313|EMBL:ARF74672.1};
OS   Kitasatospora albolonga.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Kitasatospora.
OX   NCBI_TaxID=68173 {ECO:0000313|EMBL:ARF74672.1, ECO:0000313|Proteomes:UP000192251};
RN   [1] {ECO:0000313|EMBL:ARF74672.1, ECO:0000313|Proteomes:UP000192251}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 101047 {ECO:0000313|EMBL:ARF74672.1,
RC   ECO:0000313|Proteomes:UP000192251};
RA   Yin M., Jiang Y.;
RT   "The complete genome sequence of Streptomyces albolongus YIM 101047,
RT   the producer of novel bafilomycins and novel odoriferous
RT   sesquiterpenoids.";
RL   Submitted (APR-2017) 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; CP020563; ARF74672.1; -; Genomic_DNA.
DR   KEGG; kab:B7C62_22380; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000192251; 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:UP000192251};
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:UP000192251}.
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   395 AA;  40927 MW;  5B8C3D3A808E6612 CRC64;
     MNETASLRAR AEIDLAALRA NVRALRERAA GAQLMAVVKS DGYGHGAVPV ARAAREAGAT
     WLGTATPHEA LALRAAGLDG PIMCWLWTPG GPWREAVEAG IDVSVSALWA LREAVAAATA
     AGRPARVQLK ADTGLGRNGC QPADWPELVA EARTAERTGA IRITGLWSHF ACADEPGHPS
     IAAQLSAFRD MVAYAEKEGV DPEVRHLANS PATLTLPEAH FDLVRTGIAM YGVSPAPELG
     TPAELGLRPV MTLAAAVALV KDVPAGHGVS YGHHYATPAE TTLGLIPVGY ADGIPRHASG
     RGPVLVGGRV RTAAGRVAMD QFVVDLGGDR PEPGAEAVLF GPGDRGEPTV EDWAVAAGTI
     GYEIVTRIGS RVPRVYVNET AGPEGPAHPS GGTAR
//
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