ID A9HXY3_BORPD Unreviewed; 620 AA.
AC A9HXY3;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Urea amidolyase subunit 1 {ECO:0000313|EMBL:CAP40626.1};
DE EC=6.3.4.6 {ECO:0000313|EMBL:CAP40626.1};
GN Name=uahA {ECO:0000313|EMBL:CAP40626.1};
GN OrderedLocusNames=Bpet0294 {ECO:0000313|EMBL:CAP40626.1};
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP40626.1, ECO:0000313|Proteomes:UP000001225};
RN [1] {ECO:0000313|EMBL:CAP40626.1, ECO:0000313|Proteomes:UP000001225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC {ECO:0000313|Proteomes:UP000001225};
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
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DR EMBL; AM902716; CAP40626.1; -; Genomic_DNA.
DR AlphaFoldDB; A9HXY3; -.
DR STRING; 94624.Bpet0294; -.
DR KEGG; bpt:Bpet0294; -.
DR eggNOG; COG0154; Bacteria.
DR Proteomes; UP000001225; Chromosome.
DR GO; GO:0004847; F:urea carboxylase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.20.58.1700; -; 1.
DR Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR Gene3D; 3.10.490.10; Gamma-glutamyl cyclotransferase-like; 1.
DR InterPro; IPR014085; Allophanate_hydrolase.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR NCBIfam; TIGR02713; allophanate_hyd; 1.
DR PANTHER; PTHR11895:SF169; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE; 1.
DR PANTHER; PTHR11895; TRANSAMIDASE; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:CAP40626.1}.
FT DOMAIN 72..443
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
SQ SEQUENCE 620 AA; 64958 MW; CC27BA5BEC5BBBE3 CRC64;
MKANDVISQP QGWTLAEWQA AYRRGAQPAD LLGRLIDSLD PGDPAWICRA DAPRLQTQLS
DLARLLDSAG GDVARLPLYG VPFAIKDNID AAGWPTTAAC PAFSYLAQQD ADVVRRLRAA
GAILIGKTNL DQFATGLVGT RSPHGAVPNT FDPAYISGGS SSGSASVVAR GLAAFALGTD
TAGSGRVPAG FNNIVGLKPT KGWLSTRGVV PACRTLDCVS IFALTVNDAD AVAMAAGGLD
PQDPYSRAAP AMPGGLPRQP KLAIPAQPEF FGDAQAQAAY DASLQVLRNM GATLQAVDFS
VFRELADLLY QGPWVAERYA AVRSLYERAP GEIDPVVRGI IEQAAQYNAV DAFEAEYQRA
ELARRIQQCL AGFDAMVVPT APSIYTIAQL RADPVALNTR LGTYTNFANL ADLSALALPG
GLRADGLPSG ITLIGPAWHD RALAEFGRRW EAAQGGTLGA TGRDRRAAIA EAANTVPAAS
AGTPVQVAVV GAHLQGMPLN HQLTSRGARF LEATQSAAAY RLYALAGSTP PKPGLVHTGD
GAAIALEVWE LAPAAFGEFV AEIPAPLGIG TLELIDGRTV KGFICEPRGI AGARDITEFG
GWRAYLRHLQ DAAAHQGEKS
//
