ID A0A0S2JJG8_9GAMM Unreviewed; 323 AA.
AC A0A0S2JJG8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:ALO36116.1};
GN ORFNames=CMT41_16295 {ECO:0000313|EMBL:ALO36116.1};
OS Colwellia sp. MT41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=58049 {ECO:0000313|EMBL:ALO36116.1, ECO:0000313|Proteomes:UP000065319};
RN [1] {ECO:0000313|EMBL:ALO36116.1, ECO:0000313|Proteomes:UP000065319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MT41 {ECO:0000313|EMBL:ALO36116.1,
RC ECO:0000313|Proteomes:UP000065319};
RA Kyaw T.S., Ugalde J., Peoples L., Narasingarao P., Chastain R.A.,
RA Yayanos A., Methe B.A., Bartlett D.H.;
RT "Distinctive Gene and Protein Characteristics of Extremely Piezophilic
RT Colwellia.";
RL Submitted (NOV-2015) 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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP013145; ALO36116.1; -; Genomic_DNA.
DR RefSeq; WP_057182795.1; NZ_CP013145.1.
DR AlphaFoldDB; A0A0S2JJG8; -.
DR STRING; 58049.CMT41_16295; -.
DR KEGG; com:CMT41_16295; -.
DR OrthoDB; 9763993at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000065319; 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; SFLDG01216; thioether_bond_formation_requi; 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 Reference proteome {ECO:0000313|Proteomes:UP000065319};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 5..229
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 323 AA; 36283 MW; 91C1AA601709DCCB CRC64;
MLTDNFGRRF YYLRLSITDV CNFSCTYCLP DGYQCDQPRD FLSLDEIKRL TKAFAELGTE
KIRITGGEPA LRKDLPKIIQ ICKETPGIKR VAITSNGFKL PEHLPQWLDA GIDAINISID
SLDPRQFHAI TGHDKLKTIL KGIDLGLADG RASIKVNTVL MREYSGKDIQ SYLDWIKDTP
ITLRFIELMQ TGDNKEFFDA QHVQGSRIKQ NLILDGWLPV IQNKSAGPAQ EFYHPDYQGK
VGLIMPYAKD FCNSCNRLRI SSSGKLHLCL FGDEGLSLRE QLQSDDIAPL QAKIVSLLGD
KKATHFLHEK LTGATKHLAM LGG
//