GenomeNet

Database: UniProt/TrEMBL
Entry: W8HAH8_RHOOP
LinkDB: W8HAH8_RHOOP
Original site: W8HAH8_RHOOP 
ID   W8HAH8_RHOOP            Unreviewed;       401 AA.
AC   W8HAH8;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   28-FEB-2018, entry version 29.
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=Pd630_LPD02830 {ECO:0000313|EMBL:AHK30053.1};
OS   Rhodococcus opacus PD630.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=543736 {ECO:0000313|EMBL:AHK30053.1, ECO:0000313|Proteomes:UP000019682};
RN   [1] {ECO:0000313|EMBL:AHK30053.1, ECO:0000313|Proteomes:UP000019682}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PD630 {ECO:0000313|EMBL:AHK30053.1,
RC   ECO:0000313|Proteomes:UP000019682};
RA   Chen Y., Ding Y., Yang L., Yu J., Liu G., Wang X., Song L., Huo L.,
RA   Yu D., Zhang S., Huo C., Wang Y., Du Y., Zhang C., Zhang H., Zhang P.,
RA   Na H., Xu S., Zhu Y., Xie Z., Zhang H., He T., Zhang Y., Wang G.,
RA   Fan Z., Yang F., Liu H., Wang X., Zhang X., Zhang M.Q., Li Y.,
RA   Steinbuechel A., Fujimoto T., Yu J., Liu P.;
RT   "Integrated omics studies delineate the formation and dynamics of
RT   lipid droplets in Rhodococcus opacus Pd630 for biofuel feedstock.";
RL   Submitted (NOV-2012) 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}.
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP003949; AHK30053.1; -; Genomic_DNA.
DR   RefSeq; WP_005239745.1; NZ_JH377098.1.
DR   EnsemblBacteria; AHK30053; AHK30053; Pd630_LPD02830.
DR   KEGG; roa:Pd630_LPD02830; -.
DR   PATRIC; fig|543736.9.peg.2791; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000019682; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000019682};
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      267    396       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     59     59       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    288    288       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     157    157       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     336    336       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      59     59       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   401 AA;  41815 MW;  E388D2191CD3A59D CRC64;
     MTLAEAVPAD DHGHSEPAAP AQAAPAPQAE AVVDLDAIAH NVRILRDSAR DAAMMAVVKA
     DGYNHGAVPV ARAALAAGAS ELGVTTVSEA LTLRRAGIDA PVLAWLHTVD ADFAPAIAAG
     VELGVSSPRH LAAVVAAARS VGVTAIVTIK VDTGLNRNGV APDELAQVLV DLARAQAEGS
     VRLRGIFSHL AHADEPHHAW IDSQRDRLVS AIADAKRQGL IPEVVHLSNS AATLTRPDLR
     FDMVRPGIAI YGLSPVPELG QFGLRPAMTL RSRVALVKKV AAGEGVSYGH QWVAPRDTTV
     ALLPFGYADG LPRSLSGRFE VQLGAERRPG IGRVCMDQVV VDLGPDGGGV REGDTAVFFG
     NGDLGEPIAQ AWADELDTIH YEVVTGVRGR TVRSYVGGTG T
//
DBGET integrated database retrieval system