ID C1DAX1_LARHH Unreviewed; 883 AA.
AC C1DAX1;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=ThiH {ECO:0000313|EMBL:ACO75310.1};
GN Name=thiH {ECO:0000313|EMBL:ACO75310.1};
GN OrderedLocusNames=LHK_02327 {ECO:0000313|EMBL:ACO75310.1};
OS Laribacter hongkongensis (strain HLHK9).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Aquaspirillaceae; Laribacter.
OX NCBI_TaxID=557598 {ECO:0000313|EMBL:ACO75310.1, ECO:0000313|Proteomes:UP000002010};
RN [1] {ECO:0000313|EMBL:ACO75310.1, ECO:0000313|Proteomes:UP000002010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLHK9 {ECO:0000313|EMBL:ACO75310.1,
RC ECO:0000313|Proteomes:UP000002010};
RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA Woo P.C., Lau S.K., Tse H., Teng J.L., Curreem S.O., Tsang A.K., Fan R.Y.,
RA Wong G.K., Huang Y., Loman N.J., Snyder L.A., Cai J.J., Huang J.D., Mak W.,
RA Pallen M.J., Lok S., Yuen K.Y.;
RT "The complete genome and proteome of Laribacter hongkongensis reveal
RT potential mechanisms for adaptations to different temperatures and
RT habitats.";
RL PLoS Genet. 5:E1000416-E1000416(2009).
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP001154; ACO75310.1; -; Genomic_DNA.
DR AlphaFoldDB; C1DAX1; -.
DR STRING; 557598.LHK_02327; -.
DR KEGG; lhk:LHK_02327; -.
DR eggNOG; COG0486; Bacteria.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_326201_0_0_4; -.
DR Proteomes; UP000002010; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044271; P:cellular nitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR GO; GO:0042364; P:water-soluble vitamin biosynthetic process; IEA:UniProt.
DR CDD; cd00880; Era_like; 1.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.40.50.11410; -; 1.
DR Gene3D; 3.40.50.11420; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR010722; BATS_dom.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR023873; FeFe-hyd_GTPase_HydF.
DR InterPro; IPR024007; FeFe-hyd_mat_HydG.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR041606; HydF_dimer.
DR InterPro; IPR040644; HydF_tetramer.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR034428; ThiH/NoCL/HydG-like.
DR NCBIfam; TIGR03918; GTP_HydF; 1.
DR NCBIfam; TIGR03955; rSAM_HydG; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43583; 2-IMINOACETATE SYNTHASE; 1.
DR PANTHER; PTHR43583:SF2; BIOTIN AND THIAMIN SYNTHESIS ASSOCIATED DOMAIN CONTAINING PROTEIN; 1.
DR Pfam; PF06968; BATS; 1.
DR Pfam; PF18128; HydF_dimer; 1.
DR Pfam; PF18133; HydF_tetramer; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01060; BATS_domain_containing; 1.
DR SFLD; SFLDG01081; cleavage_of_the_Ca-Cb_bond_in; 1.
DR SMART; SM00876; BATS; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002010};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 78..311
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 432..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 883 AA; 96073 MW; FF8EB53EC769FBD7 CRC64;
MSDLHDTQAD WLAPAAIEAA LADAVADPVR VQEILARARE LKGLDFADVA ALTLIDSAEL
CEALFATARE VKEAIYGRRM VLFAPLYISN LCKNECSYCA FRRSNKDIQR HALDMDAIRH
EARQLIDQGQ KRVLLVAGEG YPAARGGFRY VLDAIEAVYS VTHAHGNIRR LNVNVAPLEL
AQFHDLKAAE IGTYQLFQET YHRAAYARVH LGGQKTDFDW RCSAMDRAML AGIDDVGLGV
LFGLHDWRFE LLSLMQHAAH LEDRFGVGPH TISVPRIEPA EGAPLSEAPP AGVSDLDFKK
IIAILRLAVP YTGLILSTRE SAAMRREACA LGVSQISAGS RTNPGGYGAD EDSTGQFQLG
DHRSLEEVVA ELAASGYVPS FCTACYRAGR TGKDFMDLAK PGADQAQVRS QCRDHPPGIP
VRLRQPGHAA GRLAGHCRST GRHGAENAPQ RRKNARHDPR RPARHLLLRR TMLTTPRGVM
PHIGLFGCRN AGKSSWFNAL TGQERAIVSA RPGSTTDPVE KAYELLPFGP VLFVDTAGLD
DEGELGMLRV QKTRAVLARV DLVVLLVSPG GLRDEDRVVL REARARGVPY LVLVNHCDVE
RPAHDVLAAL QQEAGRCLTV SSLSDDDVAE VRQALLALLQ PPAGEPVPVL VGDLLAPQDL
VLLVVPIDIS APKGRLILPQ VMTLREVLDR DACALVVKEQ DYAARLARLD VPPALVVCDS
QVVQPVVQQT PDTVPLTTFS ILMSRFKGDM VQLAQGAGCI RRLLPGDRVL IAEACSHHAQ
DDDIGRVKIP RLLSRAANGP LEVDVVAGRD FPDDLSGYQL VVQCGGCMVT RQDMLARQRQ
AARQGVPVTN YGMAISVAQG VIERTLACFP AALEAYRQAG RQH
//
