ID A0A1Z4JQT2_LEPBY Unreviewed; 763 AA.
AC A0A1Z4JQT2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN ORFNames=NIES2135_58990 {ECO:0000313|EMBL:BAY59023.1};
OS Leptolyngbya boryana NIES-2135.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya.
OX NCBI_TaxID=1973484 {ECO:0000313|EMBL:BAY59023.1, ECO:0000313|Proteomes:UP000217895};
RN [1] {ECO:0000313|EMBL:BAY59023.1, ECO:0000313|Proteomes:UP000217895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2135 {ECO:0000313|EMBL:BAY59023.1,
RC ECO:0000313|Proteomes:UP000217895};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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; AP018203; BAY59023.1; -; Genomic_DNA.
DR RefSeq; WP_017290647.1; NZ_AP018203.1.
DR AlphaFoldDB; A0A1Z4JQT2; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000217895; 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-KW.
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; 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:UP000217895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 9..95
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 205..390
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 24
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 42
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 763 AA; 85329 MW; 3DE94D16F7986E48 CRC64;
MNDKNDLERL RIQIRGAVQG VGFRPFVYRL ATNLGMVGWI KNSAEGVWIE IEGTRSQLDL
FLLKLEQEKP VHSLIQQLQA SSLVPLDESD FEIYPSVSGE KTTIVLPDLA TCSDCIRELF
DPNNPRYRYP FINCTHCGPR FSIINALPYD RPNTSMNAFQ MCDRCRTEYE NPLDRRFHAQ
PIACPECGPR LEWWDHHGKR LASDEAALQA AIQAIQNGQI IAVKGLGGFH FMVDARNSDA
ISTLRQRKHR PDKPCAVMYP SLAAVQKDCE LSDLEAQLLT ASEAPIVLLR RKANISVLER
VAPNNAYLGV LLPYTPLHHL LLSALNFPIV ATSGNLSNEP ICIDEREAIQ RLSGIADAFL
VHNRPIVRAV DDSIVRVIAD REMILRRSRG YAPLPIALSK PVPTCLAVGG HLKNTIALTI
DSNLFVSQHI GDLENQATLK AFKQAIDTFE QLYEVHPDLI ACDDHPDYLS TQYAQHRSSK
FPSSQIFPVQ HHHAHIAACM AENGLEETVL GVAWDGTGYG LDGTIWGGEF FLANLTDFQR
VGHFKPFRLP GGEKAIREPR RAAIAVLYEL WGEAAFDRTD LTPVQAFNAQ ERDILQAMLQ
KELNTPWTSS AGRLFDAISA LLNLVQISTF EGQAAMALEF ALEHISTDEF YPSVIHQGIF
DWSTMVEEII ADIEQKTSGA MVSAKFHNTM VEVILQFARQ WKQKRVVLSG GCFQNRYFSD
RTIARLQAEG FQPYWHRHIP PNDGGIAVGQ AIIAASQLLK RGG
//