ID G2LK99_CHLTF Unreviewed; 483 AA.
AC G2LK99;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Dinucleotide-utilizing enzymes involved in molybdopterin and thiamine biosynthesis family 2 {ECO:0000313|EMBL:AEP13586.1};
GN OrderedLocusNames=Cabther_B0588 {ECO:0000313|EMBL:AEP13586.1};
OS Chloracidobacterium thermophilum (strain B).
OC Bacteria; Acidobacteriota; Blastocatellia; Chloracidobacterium.
OX NCBI_TaxID=981222 {ECO:0000313|EMBL:AEP13586.1, ECO:0000313|Proteomes:UP000006791};
RN [1] {ECO:0000313|EMBL:AEP13586.1, ECO:0000313|Proteomes:UP000006791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:AEP13586.1,
RC ECO:0000313|Proteomes:UP000006791};
RX PubMed=21951563; DOI=10.1111/j.1462-2920.2011.02592.x;
RA Garcia Costas A.M., Liu Z., Tomsho L.P., Schuster S.C., Ward D.M.,
RA Bryant D.A.;
RT "Complete genome of Candidatus Chloracidobacterium thermophilum, a
RT chlorophyll-based photoheterotroph belonging to the phylum Acidobacteria.";
RL Environ. Microbiol. 14:177-190(2012).
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DR EMBL; CP002515; AEP13586.1; -; Genomic_DNA.
DR RefSeq; WP_014101324.1; NC_016025.1.
DR AlphaFoldDB; G2LK99; -.
DR STRING; 981222.Cabther_B0588; -.
DR KEGG; ctm:Cabther_B0588; -.
DR HOGENOM; CLU_013325_1_1_0; -.
DR OrthoDB; 9800872at2; -.
DR Proteomes; UP000006791; Chromosome 2.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR CDD; cd00757; ThiF_MoeB_HesA_family; 1.
DR CDD; cd17074; Ubl_CysO_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR003749; ThiS/MoaD-like.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953:SF102; ADENYLYLTRANSFERASE AND SULFURTRANSFERASE MOCS3; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00899; ThiF; 1.
DR Pfam; PF02597; ThiS; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR SUPFAM; SSF54285; MoaD/ThiS; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006791};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 392..481
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 483 AA; 52399 MW; 550439E4D6FD9B97 CRC64;
MPVTVLIPTA LRGFAGGKAE IEVTAATAGE ALLALGNAHP ELKKHLFDEQ GAVRSFVNVY
VGDEDIRALQ GADTPVQDGD TLMIVPSIAG GAPDGDTAGR PLPELTPEEY TRYGRHLILP
EVGLEGQRKL KQARVLMVGT GGLGAPLGMY LAAAGVGTLG IVDFDVVDAS NLQRQIIHGT
KDIGRPKVAS ARDRLQDINP NVKLEIHETR LTSRNALDII REYDIVVDGT DNFPTRYLVN
DACVLLDKPN VYGSIFRFEG QASVFWGSRG PCYRCLYPEP PPPGLVPSCA EGGVLGVLPG
IVGAIQANET IKLILGAEGV LLGRLLLFDA WRMKFRELKL RKHPQCALCS DHPTIRELID
YEQFCGLKPP ASTEKPAMEE ITAVELKRRL DLGEDLQIID VREPHEYEIA RLPNSKLIPL
GEIVARRDEI DPTRTTIVHC KMGGRSARAI QALKNAGFPG ELINLAGGIT AWSNDVDPSV
PKY
//
