ID A0A1N7HF03_9ACTN Unreviewed; 786 AA.
AC A0A1N7HF03;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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 ORFNames=SAMN05421833_14626 {ECO:0000313|EMBL:SIS23270.1};
OS Microbispora rosea.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=58117 {ECO:0000313|EMBL:SIS23270.1, ECO:0000313|Proteomes:UP000186096};
RN [1] {ECO:0000313|EMBL:SIS23270.1, ECO:0000313|Proteomes:UP000186096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12950 {ECO:0000313|EMBL:SIS23270.1,
RC ECO:0000313|Proteomes:UP000186096};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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; FTNI01000046; SIS23270.1; -; Genomic_DNA.
DR RefSeq; WP_076442767.1; NZ_FTNI01000046.1.
DR AlphaFoldDB; A0A1N7HF03; -.
DR STRING; 58117.SAMN05421833_14626; -.
DR OrthoDB; 9808093at2; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000186096; 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; 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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 5..91
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 200..389
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 20
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 38
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 786 AA; 83302 MW; 6EA705F930E66199 CRC64;
MSRRAVAVRI EGIVQGVGFR PFVYGLATRL GLAGLVGNDE RGVFIEVEGG SAPVEEFLAA
LTGDPPPLAV IERITTGPAP VTGRRTFAIA PSAAGGDRHA LVSPDVATCD ACLRDLTDPA
DRRCGYAFTN CTGCGPRFTI VRDVPYDRAN TTMAGFRMCA DCAGEYHDPG DRRFHAQPVC
CPACGPSLRF HGPGGSGAAG DPLEPAVRLL REGGVLAVKG LGGYHLAALA ADEPAVAALR
SRKHREDKPF AVMAGDVAAA RRLCVVDPAE ERLLTGPARP VVLLRRLPDA SVAPSVAPSV
APGNRWLGVL LPYTPLHHLL LRSLGQPIVL TSGNVSDEPI AYRDEDALER LGGIADAFLT
HDRPIHIRTD DSVVRVFRGR DLPIRRSRGY VPHPLPLARA ARRPVLACGA ELKHTFCLVK
DDRAFVSHHI GDLENYETLR SFTEGVDHFR RLFDITPEVV AHDLHPDYLS TKWALDQDAD
LVGVQHHHAH IASCLADNGV AGPVAGVAFD GLGYGSDGTL WGGEFLVADL AGFERAGHLA
PVPMPGGATA IRQPWRMAAA YLDLAYDGDV PEDLDVVRRN AGQWAAVVAL ARRGVNAPLT
SSMGRLFDAV AAVAGVRDAI TYEGQAAVEF EQLADPAVDD AYPCGLVSAG TRFAVPGVEL
VRAVADDLRA CVPRDVVAAR FHNAVARVVA DGCTLVRKAC GLSTVALSGG VFQNLLLLGR
AVTLLEERGF TVLTHHRVPP NDGGVSLGQA AVAAAAMAAN SPIRGVRREL SQARHTWFGG
MSETGT
//
