ID I2B3Z3_SHIBC Unreviewed; 760 AA.
AC I2B3Z3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Carbamoyltransferase HypF {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN Name=hypF {ECO:0000313|EMBL:AFJ45247.1};
GN OrderedLocusNames=EBL_c01110 {ECO:0000313|EMBL:AFJ45247.1};
OS Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 /
OS CDC 9005-74) (Escherichia blattae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shimwellia.
OX NCBI_TaxID=630626 {ECO:0000313|EMBL:AFJ45247.1, ECO:0000313|Proteomes:UP000001955};
RN [1] {ECO:0000313|EMBL:AFJ45247.1, ECO:0000313|Proteomes:UP000001955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74
RC {ECO:0000313|Proteomes:UP000001955};
RX PubMed=22843577; DOI=10.1128/JB.00829-12;
RA Brzuszkiewicz E., Waschkowitz T., Wiezer A., Daniel R.;
RT "Complete genome sequence of the B12-producing Shimwellia blattae strain
RT DSM 4481, isolated from a cockroach.";
RL J. Bacteriol. 194:4436-4436(2012).
CC -!- FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Along with
CC HypE, it catalyzes the synthesis of the CN ligands of the active site
CC iron of [NiFe]-hydrogenases. HypF functions as a carbamoyl transferase
CC using carbamoylphosphate as a substrate and transferring the
CC carboxamido moiety in an ATP-dependent reaction to the thiolate of the
CC C-terminal cysteine of HypE yielding a protein-S-carboxamide.
CC {ECO:0000256|PIRNR:PIRNR006256}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + C-terminal L-cysteinyl-[HypE protein] + carbamoyl
CC phosphate + H2O = AMP + C-terminal S-carboxamide-L-cysteinyl-[HypE
CC protein] + diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:55636,
CC Rhea:RHEA-COMP:14247, Rhea:RHEA-COMP:14392, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:76913,
CC ChEBI:CHEBI:139126, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000256|ARBA:ARBA00001186,
CC ECO:0000256|PIRNR:PIRNR006256};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00520};
CC -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC {ECO:0000256|ARBA:ARBA00004711, ECO:0000256|PIRNR:PIRNR006256}.
CC -!- SIMILARITY: Belongs to the carbamoyltransferase HypF family.
CC {ECO:0000256|ARBA:ARBA00008097, ECO:0000256|PIRNR:PIRNR006256}.
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; CP001560; AFJ45247.1; -; Genomic_DNA.
DR AlphaFoldDB; I2B3Z3; -.
DR STRING; 630626.EBL_c01110; -.
DR KEGG; ebt:EBL_c01110; -.
DR PATRIC; fig|630626.3.peg.116; -.
DR eggNOG; COG0068; Bacteria.
DR HOGENOM; CLU_009164_0_0_6; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000001955; Chromosome.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.110.120; -; 1.
DR Gene3D; 3.30.420.360; -; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 3.90.870.30; -; 1.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR017968; Acylphosphatase_CS.
DR InterPro; IPR004421; Carbamoyltransferase_HypF.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR041440; HypF_C.
DR InterPro; IPR006070; Sua5-like_dom.
DR InterPro; IPR011125; Znf_HypF.
DR NCBIfam; TIGR00143; hypF; 1.
DR PANTHER; PTHR42959; CARBAMOYLTRANSFERASE; 1.
DR PANTHER; PTHR42959:SF1; CARBAMOYLTRANSFERASE HYPF; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR Pfam; PF17788; HypF_C; 1.
DR Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR Pfam; PF07503; zf-HYPF; 2.
DR PIRSF; PIRSF006256; CMPcnvr_hdrg_mat; 1.
DR SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR SUPFAM; SSF55821; YrdC/RibB; 1.
DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
DR PROSITE; PS51163; YRDC; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001955};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 22..106
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 214..390
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 37
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 55
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 760 AA; 81632 MW; 0AA3EEA245368C49 CRC64;
MGRVSSRVFF ISSANITMRN QGVALRIRGK VQGVGFRPYI WQIASEMGLA GDVCNDGSGV
VIRLVHLPED FITALYQRCP PLARIDSLER SVMHWPALPD DFTIRQSDAG AMSTQIVPDA
ATCPACLAEM NDPAERRYRY PFINCTHCGP RFTIIRAMPY DRPFTVMAGF PLCAACEAEY
RDPRDRRFHA QPVACPACGP WLSWQAGDQH AEREAALQAA LAALRGGQII AVKGVGGFHL
VCDARNDTAV TLLRLRKQRP KKPLAVMLAQ DSGLPGAACA LLNTPAAPIV LVDKAHCGPL
SPEIAPGLNE VGVLLPGNPL QHLLSQAFGG PLVMTSGNLS GRPPALTNPQ ALEDLAGLAD
GWLLHNRDIL QRMDDSLVRA DGSMLRRARG FVPDALPLPP GLTVTQPLLC LGADLKNTFA
LARGDQLVLS QHLGDLGQEG VEEQWQHALD LMRQVYDFTP QQVVMDAHPG YQLTRIGHQM
GLPVHLVLHH HAHIAACLAE HHWPLDGGAV IGLALDGIGM GAEGELWGGE CLRVDYRQCD
KLGGLPAVAL PGGDLAARQP WRNLLAHCLR FVPGWEALPE TAVIRQQMWQ PLAKAIARGV
NAPLASSAGR LFDAAAAALG CVGLAQSYEG EAACTLEAMA WRHGPVDHPV SLPCVDGQLD
LAVFWQSWLG WQAAPEARAW AFHDALAAGL AALARYHARQ QGLNTVACGG GVWHNRLLSQ
RLGHHLADCT LLFPHILPAG DGAISAGQAV IAAAWSQAKG
//
