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Database: UniProt
Entry: A0A346NKE3_9ALTE
LinkDB: A0A346NKE3_9ALTE
Original site: A0A346NKE3_9ALTE 
ID   A0A346NKE3_9ALTE        Unreviewed;       322 AA.
AC   A0A346NKE3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, 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   Name=moaA {ECO:0000313|EMBL:AXR06000.1};
GN   ORFNames=D0Y50_06155 {ECO:0000313|EMBL:AXR06000.1};
OS   Salinimonas sediminis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Salinimonas.
OX   NCBI_TaxID=2303538 {ECO:0000313|EMBL:AXR06000.1, ECO:0000313|Proteomes:UP000262073};
RN   [1] {ECO:0000313|EMBL:AXR06000.1, ECO:0000313|Proteomes:UP000262073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N102 {ECO:0000313|EMBL:AXR06000.1,
RC   ECO:0000313|Proteomes:UP000262073};
RA   Cao J.;
RT   "Salinimonas sediminis sp. nov., a piezophilic bacterium isolated from a
RT   deep-sea sediment sample from the New Britain Trench.";
RL   Submitted (AUG-2018) 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; CP031769; AXR06000.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A346NKE3; -.
DR   KEGG; salm:D0Y50_06155; -.
DR   OrthoDB; 9763993at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000262073; Chromosome.
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   CDD; cd21117; Twitch_MoaA; 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:SF28; GTP 3',8-CYCLASE; 1.
DR   PANTHER; PTHR22960; MOLYBDOPTERIN COFACTOR SYNTHESIS PROTEIN A; 1.
DR   Pfam; PF06463; Mob_synth_C; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDG01383; cyclic_pyranopterin_phosphate; 1.
DR   SFLD; SFLDG01386; main_SPASM_domain-containing; 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..228
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   322 AA;  35789 MW;  00B761B9851672D2 CRC64;
     MLEDSFGRRF HYLRLSITEA CNFRCQYCLP DGYDGPPNSA FLNIHEIQTL LTAFAQMGTS
     KVRITGGEPS LRRDFTDIIA ATANTPGINR IAATSHGARL AKDAHRWAQA GLHQVNVSID
     SLDPNQFALI TGQDKLKQIL NGLDVAVEAG LNVKINTVLL QDFSSNRLQR FLTWLKTTPV
     TLRFIELMET GEHHNFFNQQ HMSGAPLRDK LLAEGWQPII RRRDAGPAQE FCHPDYAGNI
     GLIMPYSKDF CESCNRLRVA ASGKLHLCLF SEQGLDLRHY LSAGDVEGVK QFVTESLGDK
     HISHYLQQGS TGATKHLAML GG
//
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