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Database: UniProt/TrEMBL
Entry: A0A076PL65_COMTE
LinkDB: A0A076PL65_COMTE
Original site: A0A076PL65_COMTE 
ID   A0A076PL65_COMTE        Unreviewed;       368 AA.
AC   A0A076PL65;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-SEP-2017, entry version 21.
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=O987_00935 {ECO:0000313|EMBL:AIJ44385.1};
OS   Comamonas testosteroni TK102.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=1392005 {ECO:0000313|EMBL:AIJ44385.1, ECO:0000313|Proteomes:UP000028782};
RN   [1] {ECO:0000313|EMBL:AIJ44385.1, ECO:0000313|Proteomes:UP000028782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TK102 {ECO:0000313|EMBL:AIJ44385.1};
RX   PubMed=25212615;
RA   Fukuda K., Hosoyama A., Tsuchikane K., Ohji S., Yamazoe A., Fujita N.,
RA   Shintani M., Kimbara K.;
RT   "Complete Genome Sequence of Polychlorinated Biphenyl Degrader
RT   Comamonas testosteroni TK102 (NBRC 109938).";
RL   Genome Announc. 2:e00865-14(2014).
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; CP006704; AIJ44385.1; -; Genomic_DNA.
DR   RefSeq; WP_043370505.1; NZ_CP006704.1.
DR   EnsemblBacteria; AIJ44385; AIJ44385; O987_00935.
DR   GeneID; 31562971; -.
DR   KEGG; ctes:O987_00935; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000028782; 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; -; 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; 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:UP000028782};
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}.
FT   DOMAIN      235    364       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    256    256       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     130    130       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     304    304       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      35     35       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   368 AA;  40362 MW;  F37FB12C8AB2A33C CRC64;
     MPRPITVTIH PEAVRHNLER VRQAVPDAKL WSVIKANAYG HGIENVFEGL RATDGFAMLD
     LDEAQRVRQL GWRGPILLLE GVFELRDLEI CSRLGIWHAV HCDEQIDWLA AHKTQVGHRV
     FLKMNSGMNR LGFTPERFRA AYARLNALPQ VDEISFMTHF SDADVEHGID HQLKVFHETT
     LDLPGERSIS NSAATLLYGD ESNVRCDWVR PGIVLYGSSP DFPAHDAAHW GLEPTMTLSS
     KIIGIQELQP GDTVGYGSRF QCDAPLRLGV VACGYADGYP RVCPTGTPVL VEGVRTRTLG
     RVSMDMMAVD LSPVPKARLG SEVTLWGRAS NGAVLPIDEV AAAAGTLGYE LMCAVAPRVP
     KLVEGAGR
//
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