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Database: UniProt
Entry: I5CR45_9BURK
LinkDB: I5CR45_9BURK
Original site: I5CR45_9BURK 
ID   I5CR45_9BURK            Unreviewed;       563 AA.
AC   I5CR45;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   13-SEP-2023, entry version 30.
DE   SubName: Full=Formylmethanofuran dehydrogenase subunit A {ECO:0000313|EMBL:EIM98363.1};
GN   ORFNames=WQE_24687 {ECO:0000313|EMBL:EIM98363.1};
OS   Paraburkholderia hospita BS001.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1171375 {ECO:0000313|EMBL:EIM98363.1};
RN   [1] {ECO:0000313|EMBL:EIM98363.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS001 {ECO:0000313|EMBL:EIM98363.1};
RX   PubMed=22843604; DOI=10.1128/JB.00725-12;
RA   Nazir R., Hansen M.A., Sorensen S., van Elsas J.D.;
RT   "Draft Genome Sequence of the Soil Bacterium Burkholderia terrae Strain
RT   BS001, Which Interacts with Fungal Surface Structures.";
RL   J. Bacteriol. 194:4480-4481(2012).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIM98363.1}.
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DR   EMBL; AKAU01000125; EIM98363.1; -; Genomic_DNA.
DR   AlphaFoldDB; I5CR45; -.
DR   PATRIC; fig|1171375.3.peg.5082; -.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR012027; Formylmethanofuran_DH_asu.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR03121; one_C_dehyd_A; 1.
DR   PANTHER; PTHR11647:SF1; COLLAPSIN RESPONSE MEDIATOR PROTEIN; 1.
DR   PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   PIRSF; PIRSF006453; FwdA; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
FT   DOMAIN          45..486
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   563 AA;  61616 MW;  E739458C497D1F75 CRC64;
     MSTFRLRGGR VYDPASRIAG QISDICVRDG RIVDLPEQES VDCEYDASGM VIMAGGIDMH
     SHIGGGKVNL ARLLMPEDHR GRRASDNPLE LASCGDCTPG TLATGYRYAE MGYTAAFEPA
     MIASNARHTH LEMGDTPIID HGAYVMLGND ELFLRMLAGH TDYERLRDYV GWSIHATRAL
     GVKVVNPGGI SAFKFNQRSL DVDEHHTHYG ITPRDVLHVL ARALTDLGVP HPLHIHASNL
     GVPGNIDSTL VTIDALEGLP GHLTHIQFHS YGNDGPRKFS SAAHRIAEAV NANPNISIDV
     GQIMFGQTVT ASGDIMKQVK QAAFASPRKW IAGDIECDAG CGVVPFRYRE TSYVNALQWT
     IGLELFLLVN NPWQITLTTD HPNGGPFTSY PHLIRLLMDK SFRDEQLAKL HPDVAAQSPL
     VSLKRELDLN EIAILTRAAP ARLLGLKDRG RLDAGAAADI AVYREHADRE AMFRAPVYVF
     KDGELVARDG RIVATPVGGT HYVEPEFDRS IEKVVEEYGD AYLATNMRRA PISRDELCLC
     GNGGRLLPAA CGVHRQQRAE SPS
//
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