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Database: UniProt
Entry: A0A2C9STJ6_9MYCO
LinkDB: A0A2C9STJ6_9MYCO
Original site: A0A2C9STJ6_9MYCO 
ID   A0A2C9STJ6_9MYCO        Unreviewed;       777 AA.
AC   A0A2C9STJ6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE            EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN   Name=hypF {ECO:0000313|EMBL:GAY15033.1};
GN   ORFNames=MSZK_17590 {ECO:0000313|EMBL:GAY15033.1};
OS   Mycobacterium sp. shizuoka-1.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=2039281 {ECO:0000313|EMBL:GAY15033.1, ECO:0000313|Proteomes:UP000223528};
RN   [1] {ECO:0000313|EMBL:GAY15033.1, ECO:0000313|Proteomes:UP000223528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=shizuoka-1 {ECO:0000313|Proteomes:UP000223528};
RA   Yoshida M., Izumiyama S., Fukano H., Sugiyama K., Suzuki M., Shibayama K.,
RA   Hoshino Y.;
RT   "Draft genome sequence of Mycobacterium sp. shizuoka-1.";
RL   Submitted (OCT-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}.
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:GAY15033.1}.
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DR   EMBL; BEWG01000025; GAY15033.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C9STJ6; -.
DR   OrthoDB; 9808093at2; -.
DR   UniPathway; UPA00335; -.
DR   Proteomes; UP000223528; Unassembled WGS sequence.
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; IPR017968; Acylphosphatase_CS.
DR   InterPro; IPR043129; ATPase_NBD.
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; SSF53067; Actin-like ATPase domain; 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:UP000223528};
KW   Transferase {ECO:0000313|EMBL:GAY15033.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          4..90
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   DOMAIN          199..385
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51163"
FT   ACT_SITE        19
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        37
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   777 AA;  81740 MW;  8DCB35E2FAEDCEC6 CRC64;
     MNVRVRLDIT GVVQGVGFRP AVARIAAEFR LGGFVYNDAG SVHCELEGPA VDVEAAIAAI
     RHRPPPMARI DSIRSRRLEP NGDNCFEIVG SRSGDLSRTL IPPDIATCAD CLREMRDPKD
     RRHAHPFITC TNCGPRYTVI TDLPYDRPAT TMAGFPMCSA CAAEYHDPAD RRYHAQTVAC
     PDCGPRLSWH PGGADSTTDD PIGAAVTALR AGRIVAIKGI GGFHLACRAQ DASVVAELRR
     RKSRPAKPFA VMVADLAAAE QIAMLDEAAA AALSSPSAPI VLVARRPGAV ADEVAPGLAD
     LGVMLAYSPV HHQLFDRLGR SETLVMTSAN QGGSPIVFRE GDLSWIDGLA DAVLAHDRPI
     GVPCEDSVLM IADRDGAVPL RRSRGYAPLP VSVPGPLPDR VVLATGGDLK TTFCLMGADG
     HAHMSAHLGD MADPRTQACF EAALDHLAFM TDRTPDVIAC DMHPGYATSA WARRYARDRP
     VIAVQHHHAH AVSLLTEHRR LGTPAIAVTY DGTGYGTDGT IWGGELLAIT ETARFTRVGH
     LRPFALPGGD GAARQPARIA LDLLHRAGIG WTTDLPPVAA LDDTALHILG QQIPRGLGCV
     PTTSMGRLFD AVASLLGVCQ EVSYEGQAAV ELEHLARDGQ PSPLDFGVTA GELDPLPVIA
     GLADGLRRGT ALADLAAGFH QAVIRATAAA ATACARAAGI TVIGLTGGVF ANRILLQGLR
     SALTESGFEV LSHRIVPCND GGLALGQAAI AAATLNDAEP AAVSERIGIC ASEYPAR
//
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