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Database: UniProt/TrEMBL
Entry: B8HCF5_PSECP
LinkDB: B8HCF5_PSECP
Original site: B8HCF5_PSECP 
ID   B8HCF5_PSECP            Unreviewed;       437 AA.
AC   B8HCF5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   22-NOV-2017, entry version 73.
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=Achl_2606 {ECO:0000313|EMBL:ACL40571.1};
OS   Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 /
OS   CIP 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS   chlorophenolicus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae;
OC   Pseudarthrobacter.
OX   NCBI_TaxID=452863 {ECO:0000313|EMBL:ACL40571.1, ECO:0000313|Proteomes:UP000002505};
RN   [1] {ECO:0000313|EMBL:ACL40571.1, ECO:0000313|Proteomes:UP000002505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 /
RC   NCIMB 13794 / A6 {ECO:0000313|Proteomes:UP000002505};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Jansson J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Arthrobacter chlorophenolicus
RT   A6.";
RL   Submitted (JAN-2009) 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; CP001341; ACL40571.1; -; Genomic_DNA.
DR   ProteinModelPortal; B8HCF5; -.
DR   STRING; 452863.Achl_2606; -.
DR   EnsemblBacteria; ACL40571; ACL40571; Achl_2606.
DR   KEGG; ach:Achl_2606; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002505; 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:UP000002505};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:ACL40571.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      288    417       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     79     79       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    309    309       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     176    176       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     356    356       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      79     79       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   437 AA;  45478 MW;  4B03F58808E65CB1 CRC64;
     MPLNPPGTLR RRTSDYSAAG TPTRITSVTY PAPTGEISAA SVHDPHYERS AVIDLDAIRH
     NVRRLAAAAS PAKVMAVVKA DAYGHGAVPV ARAALEAGAS WLGVAHISEA LALRAAGIDA
     PLLAWLHTTD SNFGAAVAAG VDIGCSGWEL ERIVAAAREQ ERPARIHLKV DTGLGRNGAT
     LEYWDTLVGE AMEYQDQGLL RVVGIFSHLA VADEPERPET DHQLAAFRDA LAVAEDAGVD
     AEVRHLANTP ATLSRPDTHF DLVRVGLGIY GLSPFDGQTS AELGLRPAMA LRTKVSQCKV
     VPAGQGVSYG LHYRTAAAST LGLIPLGYAD GIPRVATGGP VRVAGTTYPV VGRIAMDQMV
     IDLGQGVQGA ALLGAEAELF GSGADGGPTA DDWARAAGTI NYEIVTRISP RVPRRFINEQ
     DTSGGGDASA AGSEGAL
//
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