ID A0A291P5W6_9GAMM Unreviewed; 801 AA.
AC A0A291P5W6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Carbamoyltransferase HypF {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN Name=hypF {ECO:0000313|EMBL:ATJ82267.1};
GN ORFNames=BEI_1280 {ECO:0000313|EMBL:ATJ82267.1};
OS Halomonas beimenensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=475662 {ECO:0000313|EMBL:ATJ82267.1, ECO:0000313|Proteomes:UP000219993};
RN [1] {ECO:0000313|EMBL:ATJ82267.1, ECO:0000313|Proteomes:UP000219993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTU-111 {ECO:0000313|EMBL:ATJ82267.1,
RC ECO:0000313|Proteomes:UP000219993};
RX PubMed=29026163;
RA Chen Y.H., Lin S.S., Shyu Y.T.;
RT "Revealing the Saline Adaptation Strategies of the Halophilic Bacterium
RT Halomonas beimenensis through High-throughput Omics and Transposon
RT Mutagenesis Approaches.";
RL Sci. Rep. 7:13037-13037(2017).
CC -!- FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Along with
CC HypE, it catalyzes the synthesis of the CN ligands of the active site
CC iron of [NiFe]-hydrogenases. HypF functions as a carbamoyl transferase
CC using carbamoylphosphate as a substrate and transferring the
CC carboxamido moiety in an ATP-dependent reaction to the thiolate of the
CC C-terminal cysteine of HypE yielding a protein-S-carboxamide.
CC {ECO:0000256|PIRNR:PIRNR006256}.
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 ECO:0000256|PIRNR:PIRNR006256};
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, ECO:0000256|PIRNR:PIRNR006256}.
CC -!- SIMILARITY: Belongs to the carbamoyltransferase HypF family.
CC {ECO:0000256|ARBA:ARBA00008097, ECO:0000256|PIRNR:PIRNR006256}.
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DR EMBL; CP021435; ATJ82267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291P5W6; -.
DR KEGG; hbe:BEI_1280; -.
DR OrthoDB; 9808093at2; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000219993; 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; 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:UP000219993};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 17..104
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 214..403
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 32
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 50
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 801 AA; 85913 MW; 472FF8C5568E766D CRC64;
MATTVTETGR QAPAACGMAI RVRGLVQGVG FRPTVWRLAR DCGLVGEVGN DAQGVWIHAW
GEASSRHRFC RRLREESPPL ARIETLEIEP LDGAPPSAGF AIVDSRGGDV HTGIVADAAT
CADCRAELFD PGDRRHRYAF TNCTHCGPRM SIVRAIPYDR ANTSMAAFPL CARCRAEYRD
PANRRFHAQP NACPECGPRL WLEGPTGASL DPGEKPLTAA RRRLRAGQIL AIKGVGGFHL
ACDATDAEAV DRLRRRKCRP DKPLALMARD LDMIRRYCRV TPREQALLES PAAPIVLLAA
GGGERLAEGV APRQRHYGFM LPYSPLHHLL LADLDAPIVL TSGNRAGEPP CIANQAARAG
LVGGEVPIAE ALLLHDREIV DRLDDSLVRT VAGAPALLRR ARGFAPAPLP LPAGFAASPP
LLALGGELKN TFCLLKDGQA ILSQHLGRLD TPEGEAARQQ TLRRYLRLFA HRPERLAIDA
HPDYRPSRAG RDWAAAHDLA LVEVQHHHAH VAACLADNGL DRDTPPALGI ALDGTGYGDD
GTLWGGEFLL ADYRGYRRLA SLMPVAMPGG TQAIRQPWRL AHAHLCRLGD WPGLAARHRR
LAFFQALEAR PLATLERMIA TGLNSPLSSA AGRLFDAVAA LLGLRLTVSY EGQAASELEA
AVEEGALAEA GYPFAIVQDE GLPRLEPGPM WQALLADLAR GETTGIMAAR FHTGLAEGLA
AMVEHLANHH GDRWGGRIAL SGGVFQNAVL AEALVPRLEA AGWKVLRHAR VPANDGGLSL
GQAAVAAALT IAETKEPSPC A
//
