ID D9QT61_ACEAZ Unreviewed; 309 AA.
AC D9QT61;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Cyclic pyranopterin monophosphate synthase {ECO:0000256|ARBA:ARBA00012575, ECO:0000256|HAMAP-Rule:MF_01224};
DE EC=4.6.1.17 {ECO:0000256|ARBA:ARBA00012575, ECO:0000256|HAMAP-Rule:MF_01224};
DE AltName: Full=Molybdenum cofactor biosynthesis protein C {ECO:0000256|HAMAP-Rule:MF_01224};
GN Name=moaC {ECO:0000256|HAMAP-Rule:MF_01224};
GN OrderedLocusNames=Acear_2071 {ECO:0000313|EMBL:ADL13561.1};
OS Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Acetohalobium.
OX NCBI_TaxID=574087 {ECO:0000313|EMBL:ADL13561.1, ECO:0000313|Proteomes:UP000001661};
RN [1] {ECO:0000313|EMBL:ADL13561.1, ECO:0000313|Proteomes:UP000001661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49924 / DSM 5501 / Z-7288
RC {ECO:0000313|Proteomes:UP000001661};
RX PubMed=21304692;
RA Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Brambilla E.,
RA Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA Bruce D., Detter C., Tapia R., Goodwin L., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M.,
RA Spring S., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Acetohalobium arabaticum type strain (Z-
RT 7288).";
RL Stand. Genomic Sci. 3:57-65(2010).
CC -!- FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-
CC dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate
CC (cPMP). {ECO:0000256|HAMAP-Rule:MF_01224}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic
CC pyranopterin phosphate + diphosphate; Xref=Rhea:RHEA:49580,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:59648, ChEBI:CHEBI:131766;
CC EC=4.6.1.17; Evidence={ECO:0000256|ARBA:ARBA00001637,
CC ECO:0000256|HAMAP-Rule:MF_01224};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046, ECO:0000256|HAMAP-Rule:MF_01224}.
CC -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000256|HAMAP-
CC Rule:MF_01224}.
CC -!- SIMILARITY: Belongs to the MoaC family. {ECO:0000256|HAMAP-
CC Rule:MF_01224}.
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DR EMBL; CP002105; ADL13561.1; -; Genomic_DNA.
DR RefSeq; WP_013279004.1; NC_014378.1.
DR AlphaFoldDB; D9QT61; -.
DR STRING; 574087.Acear_2071; -.
DR KEGG; aar:Acear_2071; -.
DR eggNOG; COG0315; Bacteria.
DR eggNOG; COG2258; Bacteria.
DR HOGENOM; CLU_078144_1_0_9; -.
DR OrthoDB; 9794429at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001661; Chromosome.
DR GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01420; MoaC_PE; 1.
DR Gene3D; 3.30.70.640; Molybdopterin cofactor biosynthesis C (MoaC) domain; 1.
DR Gene3D; 2.40.33.20; PK beta-barrel domain-like; 1.
DR HAMAP; MF_01224_B; MoaC_B; 1.
DR InterPro; IPR023045; MoaC.
DR InterPro; IPR047594; MoaC_bact/euk.
DR InterPro; IPR036522; MoaC_sf.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR NCBIfam; TIGR00581; moaC; 1.
DR PANTHER; PTHR36930; METAL-SULFUR CLUSTER BIOSYNTHESIS PROTEINS YUAD-RELATED; 1.
DR PANTHER; PTHR36930:SF1; MOSC DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01967; MoaC; 1.
DR Pfam; PF03473; MOSC; 1.
DR SUPFAM; SSF55040; Molybdenum cofactor biosynthesis protein C, MoaC; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01224};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|HAMAP-Rule:MF_01224};
KW Reference proteome {ECO:0000313|Proteomes:UP000001661}.
FT DOMAIN 181..306
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT ACT_SITE 132
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT BINDING 79..81
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT BINDING 117..118
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
SQ SEQUENCE 309 AA; 33601 MW; FB0C52A63D139C96 CRC64;
MTTEEKSFTH FNESGRAQMV DVSDKPVTSR KAVAEGRVYT SPETIERIES DGIEKGDVMG
VAQIAGIMNA KRTSEIIPMC HPLNITGVDL DFEINNEENY IRIVAEVKIS SQTGVEMEAL
TAVSTAALTI YDMCKAVDKA MEIGEIRLLK KSGGQSGNFR RGKMSEIVAV SVSESKGEQK
ENVDSAVLKE NHGLTGDAHA GDWHRQVSLL AQESIDKMNN QGLDVTAGDF AENLTTKDID
LLELDLGTRI EIGGQAVLEI TQHGKECHDR CAVYEQAGDC VMPREGIFAK VITGGEVKPG
DKIEVLDND
//
