GenomeNet

Database: UniProt/TrEMBL
Entry: A0A1A9GAZ5_9RHIZ
LinkDB: A0A1A9GAZ5_9RHIZ
Original site: A0A1A9GAZ5_9RHIZ 
ID   A0A1A9GAZ5_9RHIZ        Unreviewed;       376 AA.
AC   A0A1A9GAZ5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   22-NOV-2017, entry version 9.
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=shn_28105 {ECO:0000313|EMBL:ANH08004.1};
OS   Shinella sp. HZN7.
OG   Plasmid pshin-03 {ECO:0000313|Proteomes:UP000077495}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Shinella.
OX   NCBI_TaxID=879274 {ECO:0000313|EMBL:ANH08004.1, ECO:0000313|Proteomes:UP000077495};
RN   [1] {ECO:0000313|EMBL:ANH08004.1, ECO:0000313|Proteomes:UP000077495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HZN7 {ECO:0000313|EMBL:ANH08004.1,
RC   ECO:0000313|Proteomes:UP000077495};
RC   PLASMID=Plasmid pshin-03 {ECO:0000313|Proteomes:UP000077495};
RA   Qiu J., Lu Z.;
RT   "Complete genome sequence of the nicotine-degrading Shinella sp.
RT   strain HZN7.";
RL   Submitted (MAY-2016) 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP015739; ANH08004.1; -; Genomic_DNA.
DR   RefSeq; WP_064333837.1; NZ_CP015739.1.
DR   EnsemblBacteria; ANH08004; ANH08004; shn_28105.
DR   KEGG; shz:shn_28105; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000077495; Plasmid pshin-03.
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:UP000077495};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647};
KW   Plasmid {ECO:0000313|EMBL:ANH08004.1};
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:UP000077495}.
FT   DOMAIN      250    376       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     51     51       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     150    150       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      51     51       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   376 AA;  39119 MW;  B3C6FA3BCCE3A135 CRC64;
     MDGGIQRAST GVASVIDGAS GYLGIDLGAL ARNYEKLAAE VAPARAAAVV KADAYGLGAG
     RVAEKLYAHG CRHFFVAQFV EALRLRPLLA ADAAVFVLNG LQPGNESACA RENIVPVVNS
     LEQWHAWSGM AKALGRTLPA ALQFDTGMSR LGVPPEEGAA LAGLVSAGGI DVLFLMSHLA
     SADDAQSEQN EDQRAEMERV AAEFPGFDVC FANSGGIFLG KAYHGVLARP GIALYGGAPT
     AGRANPMEPV VSLDVAVVQT RSVPTGTRVG YGASHVTAGP ARLATIAAGY ADGLPRSLSG
     RGAAYCDGVR LPIVGRVSMD SITIDISVLP EGRLALGSRV EILGPHQSLE DVARDAGTIP
     YEILTGLGQR YRRQYR
//
DBGET integrated database retrieval system