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Database: UniProt
Entry: A0A1Z4JQT2_LEPBY
LinkDB: A0A1Z4JQT2_LEPBY
Original site: A0A1Z4JQT2_LEPBY 
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
//
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