ID Q31K38_SYNE7 Unreviewed; 770 AA.
AC Q31K38;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN OrderedLocusNames=Synpcc7942_2551 {ECO:0000313|EMBL:ABB58581.1};
OS Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS (Anacystis nidulans R2).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1140 {ECO:0000313|EMBL:ABB58581.1, ECO:0000313|Proteomes:UP000889800};
RN [1] {ECO:0000313|Proteomes:UP000889800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805
RC {ECO:0000313|Proteomes:UP000889800};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
CC -!- SIMILARITY: Belongs to the carbamoyltransferase HypF family.
CC {ECO:0000256|ARBA:ARBA00008097, ECO:0000256|PIRNR:PIRNR006256}.
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DR EMBL; CP000100; ABB58581.1; -; Genomic_DNA.
DR RefSeq; WP_011243869.1; NZ_JACJTX010000001.1.
DR AlphaFoldDB; Q31K38; -.
DR STRING; 1140.Synpcc7942_2551; -.
DR PaxDb; 1140-Synpcc7942_2551; -.
DR GeneID; 76401278; -.
DR KEGG; syf:Synpcc7942_2551; -.
DR eggNOG; COG0068; Bacteria.
DR HOGENOM; CLU_009164_0_0_3; -.
DR OrthoDB; 9808093at2; -.
DR BioCyc; SYNEL:SYNPCC7942_2551-MONOMER; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000889800; 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; 3.90.870.50; -; 1.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
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; 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:UP000889800};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 11..97
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 208..393
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 26
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 44
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 770 AA; 85148 MW; 3529A242BB7C23E5 CRC64;
MTGVLTAKQE RWRLRVQGVV QGIGFRPFVW RLARELGLTG WVNNDAAGAQ IEVEGAIAQL
QQFQQRLLVE LPAAGRCDRL QQERLTLQGD REFVIATSMA SEQSTAQLPP DRAPCSACLR
ELWDLRDRRY RYPFLNCTVC GPRASIVRQL PYDRNRTTLA TFPLCPDCQR EYQDPSDRRF
HAQPIACPTC GPQLQLWDAQ GQVLADRDRS LTEAIAALQQ GKILALKGLG GFQLLVDACQ
TDAVQRLRDR KSRPHKPLAL LLPDLEAVRQ LCQISAAEAE LLQSPAAPIV LLRAIASEPW
LAAIAPDCCE LGLMLPATPL HHLLSRDFGQ PLVATSGNRS GDPLCWDEVD ALESLSAIAD
LWLVHDRPIA LPMDDSVTRI IDGQIQVLRR ARGYVPTPIA IATPAEPLLI LGSWQKNTPA
IAADGQLQLA PYVGDLESLA ARDRRQQVIE HLQTVMGLQP TAWVADAHPD APLLAPTETR
SGWHVQHHLA HVLAVAAEHQ LQPPFLGLAW DGSGWGLDQT VWGSEALICQ TEGWQRWRHL
QLWPLLGGDR AAKEPRRSAL ALLWQLEGDR CWDLPELQTV FSPTERSLLQ AWLSRDRGLK
TSSMGRLFEA IAWICRWQGD QTYEGQVATW LENQCDPQIV GDYPLSLTET GIDWRSLLQA
VWCDRQADLS TAILATRFHR SLIQLVVALA QQAGLEPVIL SGGCFQNRFL LEGAIAALRS
AGFQPYWAQQ LPPNDGGIAA GQVLAVHWYG GSKHVLSGSG TTAQYSHAAG
//
