UniProt: A0A0F7HAQ6

Database: UniProt
Entry: A0A0F7HAQ6_SERFO

LinkDB:  A0A0F7HAQ6_SERFO 
Original site:  A0A0F7HAQ6_SERFO

All links

Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (7)   
   InterPro (6)   
   Pfam (1)   
All databases (17)   

Download RDF

ID   A0A0F7HAQ6_SERFO        Unreviewed;       376 AA.
AC   A0A0F7HAQ6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=dTDP-4-amino-4,6-dideoxygalactose transaminase {ECO:0000256|HAMAP-Rule:MF_02026};
DE            EC=2.6.1.59 {ECO:0000256|HAMAP-Rule:MF_02026};
GN   Name=wecE {ECO:0000256|HAMAP-Rule:MF_02026};
GN   ORFNames=BSQ40_13015 {ECO:0000313|EMBL:OKP28121.1}, CRN79_09075
GN   {ECO:0000313|EMBL:ATM75976.1}, WN53_09240
GN   {ECO:0000313|EMBL:AKG69279.1};
OS   Serratia fonticola.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=47917 {ECO:0000313|EMBL:AKG69279.1, ECO:0000313|Proteomes:UP000034699};
RN   [1] {ECO:0000313|EMBL:AKG69279.1, ECO:0000313|Proteomes:UP000034699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4576 {ECO:0000313|EMBL:AKG69279.1,
RC   ECO:0000313|Proteomes:UP000034699};
RA   Chan K.-G., Ee R.;
RT   "Complete Genome Sequencing of Serratia Fonticola DSM-4576.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OKP28121.1, ECO:0000313|Proteomes:UP000186436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5l {ECO:0000313|EMBL:OKP28121.1,
RC   ECO:0000313|Proteomes:UP000186436};
RA   Goncharov A., Grigoriev S., Azarov D., Kolodzhieva V., Tikhonov A.,
RA   Akhremenko Y., Tarasova L., Zueva L., Suvorov A.;
RT   "Draft genome sequence of Serratia fonticola 5l isolated from intestinal
RT   tract content of a 9000-year-old elk (Alces alces) from permafrost on the
RT   Omoloy river.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000221800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_411 {ECO:0000313|Proteomes:UP000221800};
RA   Goldberg B., Campos J., Tallon L., Sadzewicz L., Ott S., Zhao X.,
RA   Nagaraj S., Vavikolanu K., Aluvathingal J., Nadendla S., Geyer C.,
RA   Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ATM75976.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FDAARGOS_411 {ECO:0000313|EMBL:ATM75976.1};
RA   Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.J.,
RA   Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA   Nadendla S., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of dTDP-4-amino-4,6-dideoxy-D-
CC       galactose (dTDP-Fuc4N) from dTDP-4-keto-6-deoxy-D-glucose (dTDP-D-
CC       Glc4O) and L-glutamate. {ECO:0000256|HAMAP-Rule:MF_02026}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose =
CC         dTDP-4-dehydro-6-deoxy-alpha-D-glucose + L-glutamate;
CC         Xref=Rhea:RHEA:10368, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57649, ChEBI:CHEBI:68492; EC=2.6.1.59;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02026};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02026};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC       antigen biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02026}.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000256|HAMAP-
CC       Rule:MF_02026, ECO:0000256|RuleBase:RU004508}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP011254; AKG69279.1; -; Genomic_DNA.
DR   EMBL; CP023956; ATM75976.1; -; Genomic_DNA.
DR   EMBL; MQRH01000010; OKP28121.1; -; Genomic_DNA.
DR   RefSeq; WP_024484180.1; NZ_MQRH01000010.1.
DR   AlphaFoldDB; A0A0F7HAQ6; -.
DR   STRING; 47917.AV650_01745; -.
DR   GeneID; 30320343; -.
DR   KEGG; sfw:WN53_09240; -.
DR   PATRIC; fig|47917.8.peg.1925; -.
DR   UniPathway; UPA00566; -.
DR   Proteomes; UP000034699; Chromosome.
DR   Proteomes; UP000186436; Unassembled WGS sequence.
DR   Proteomes; UP000221800; Chromosome.
DR   GO; GO:0019180; F:dTDP-4-amino-4,6-dideoxygalactose transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00616; AHBA_syn; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_02026; WecE_RffA; 1.
DR   InterPro; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR032894; WecE.
DR   InterPro; IPR012749; WecE-like.
DR   NCBIfam; TIGR02379; ECA_wecE; 1.
DR   PANTHER; PTHR30244:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:AKG69279.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02026,
KW   ECO:0000256|PIRSR:PIRSR000390-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034699};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02026, ECO:0000313|EMBL:AKG69279.1}.
FT   ACT_SITE        181
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         181
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02026,
FT                   ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   376 AA;  41863 MW;  5795B8A6378BAC1C CRC64;
     MIPFNAPPVV GTELDYMQAA MSSGKLCGDG GFTRRCQQWM EQHFGCPKVL LTPSCTASLE
     MAAILLDIQP GDEVIMPSYT FVSTANAFVL RGAVMVFVDL RPDTMNIDET KIEAAITDKT
     RAIVPVHYAG VACEMDTIMA LAKKYNLMVV EDAAQGVMST YKGKALGTIG HIGCFSFHET
     KNYTAGGEGG ATLINDPALI DRAEVIREKG TNRSQFFRGQ VDKYTWRDIG SSYLMSDLQA
     AYLWAQLEAA ETINQRRLKL WQNYYDALKP LAAAGRIALP VIPANCVHNA HMFYIKLKDV
     QDRTAFIDYL KEAEIMSVFH YIPLHACPAG EKFGRFSGED RFTTKESERL VRLPLFFNMS
     DVNQRTVINT ILSFLA
//

DBGET integrated database retrieval system