GenomeNet

Database: UniProt
Entry: A0A0S2JJG8_9GAMM
LinkDB: A0A0S2JJG8_9GAMM
Original site: A0A0S2JJG8_9GAMM 
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
//
DBGET integrated database retrieval system