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Database: UniProt
Entry: A0A1H4CTB8_9BACT
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ID   A0A1H4CTB8_9BACT        Unreviewed;       321 AA.
AC   A0A1H4CTB8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=GTP 3',8-cyclase {ECO:0000256|ARBA:ARBA00012167};
DE            EC=4.1.99.22 {ECO:0000256|ARBA:ARBA00012167};
GN   ORFNames=SAMN05660909_02769 {ECO:0000313|EMBL:SEA63352.1};
OS   Chitinophaga terrae (ex Kim and Jung 2007).
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=408074 {ECO:0000313|EMBL:SEA63352.1, ECO:0000313|Proteomes:UP000199656};
RN   [1] {ECO:0000313|Proteomes:UP000199656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23920 {ECO:0000313|Proteomes:UP000199656};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-
CC         dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-
CC         methionine; Xref=Rhea:RHEA:49576, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:131766; EC=4.1.99.22;
CC         Evidence={ECO:0000256|ARBA:ARBA00000034};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR   EMBL; FNRL01000011; SEA63352.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4CTB8; -.
DR   STRING; 408074.SAMN05660909_02769; -.
DR   OrthoDB; 9763993at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000199656; Unassembled WGS sequence.
DR   GO; GO:0019008; C:molybdopterin synthase complex; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0061798; F:GTP 3',8'-cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR013483; MoaA.
DR   InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR   InterPro; IPR010505; MoaA_twitch.
DR   InterPro; IPR007197; rSAM.
DR   NCBIfam; TIGR02666; moaA; 1.
DR   PANTHER; PTHR22960:SF0; MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN 1; 1.
DR   PANTHER; PTHR22960; MOLYBDOPTERIN COFACTOR SYNTHESIS PROTEIN A; 1.
DR   Pfam; PF13353; Fer4_12; 1.
DR   Pfam; PF06463; Mob_synth_C; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDG01383; cyclic_pyranopterin_phosphate; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   4: Predicted;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          5..230
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   321 AA;  35286 MW;  1610E40523533870 CRC64;
     MLLDAQQRVI NYVRLSVTDR CNLRCTYCMP ADMKFAKKDT LLTDEEIITV LSTLAAAGVS
     KVRITGGEPF LRPGLLSLLE KIHNIEGIAN IAVTTNGVLT SDYIPALKKL GADHINLSLD
     TLQADRFIKI TRRDSFAAVI KTFDSLLAHQ LQVKINMVVM DNVNTDEIND FVALTKDAPV
     SVRFIEEMPF NGQGHGFSGI NWNYHRILET ISVQYQLQKL SDAPNTTSIN YRIPGHQGSI
     GVIPAYSRTF CGSCNRLRIA ANGGVRTCLY GNDVLNLKKL INTGQPLMPA IIDALNARYA
     DGFEAEKHAS LDKASMSLIG G
//
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