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Database: UniProt/TrEMBL
Entry: A0A0U3DSF7_9BURK
LinkDB: A0A0U3DSF7_9BURK
Original site: A0A0U3DSF7_9BURK 
ID   A0A0U3DSF7_9BURK        Unreviewed;       370 AA.
AC   A0A0U3DSF7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=AT984_20055 {ECO:0000313|EMBL:ALT79140.1};
OS   Paucibacter sp. KCTC 42545.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Paucibacter.
OX   NCBI_TaxID=1768242 {ECO:0000313|EMBL:ALT79140.1, ECO:0000313|Proteomes:UP000056576};
RN   [1] {ECO:0000313|EMBL:ALT79140.1, ECO:0000313|Proteomes:UP000056576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 42545 {ECO:0000313|EMBL:ALT79140.1,
RC   ECO:0000313|Proteomes:UP000056576};
RA   Kim S.-G., Lee Y.-J.;
RT   "Complete genome of Paucibacter sp. KCTC 42545.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC       also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC       from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
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DR   EMBL; CP013692; ALT79140.1; -; Genomic_DNA.
DR   RefSeq; WP_058721614.1; NZ_CP013692.1.
DR   AlphaFoldDB; A0A0U3DSF7; -.
DR   STRING; 1768242.AT984_20055; -.
DR   KEGG; pkt:AT984_20055; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000056576; 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   CDD; cd06827; PLPDE_III_AR_proteobact; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 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   NCBIfam; TIGR00492; alr; 1.
DR   PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR   PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
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; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000056576}.
FT   DOMAIN          233..362
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        35
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        254
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         302
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         35
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   370 AA;  40244 MW;  1966FB4AC8C09D6D CRC64;
     MPRPIEAHIH LPAIAHNLAR ARARAPDAKL WAVVKANAYG HGIAHAYEAM RSADGFALLD
     FAEAKLLREL GWRGPILLLE GCFEARDLEL CSRLKLWHTV HCEQQIDWLA MHKTHEPHRV
     FLKLNSGMNR LGFTPQAFRA AWTRLNVLPQ VDEISLMTHF SDADGEIGIE AQVAAFERVC
     ADLPGERSLS NSAAILRHSE RLRSDWVRAG ILTYGGVPDY PVHDQGFWDL QPAMSLRSKI
     IAVQHLQPGD TVGYGSSFTA TAPMRIGVVA CGYADGYPRH CPTGTPVLVD GQRCSTVGRV
     SMDMLAVDLT ALPKAGAGSE VTLWGRSSKG QVLPIDEVAQ AAKTIGYELM CALALRVPVT
     VDHGAAGLAG
//
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