ID A0A1Q6Y0B6_9CHLR Unreviewed; 395 AA.
AC A0A1Q6Y0B6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Molybdopterin biosynthesis protein MoeB {ECO:0000313|EMBL:OLB31372.1};
GN ORFNames=AUH05_19585 {ECO:0000313|EMBL:OLB31372.1};
OS Ktedonobacter sp. 13_2_20CM_53_11.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805233 {ECO:0000313|EMBL:OLB31372.1, ECO:0000313|Proteomes:UP000185646};
RN [1] {ECO:0000313|EMBL:OLB31372.1, ECO:0000313|Proteomes:UP000185646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLB31372.1}.
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DR EMBL; MNDA01000560; OLB31372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q6Y0B6; -.
DR Proteomes; UP000185646; Unassembled WGS sequence.
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; cd00158; RHOD; 1.
DR CDD; cd00757; ThiF_MoeB_HesA_family; 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; 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; 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 SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 37..127
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 395 AA; 43089 MW; 4153A64A0F634ECC CRC64;
MGEASREIMR QARRQVPEWS TPQVNEAMAH QHEAGRENQE IVLVDVREKH EWNEGHIPGA
IHVPRGYLEL QVEEAVPDKD KTVVLYCAGG VRSLMAGATL QQMGYKNVVS MAGGFGAWKG
NGYSFVQPRT MSEAQAKRYS RHLLVPEVGE EGQFKLLDSR VLLIGAGGLG SPAAYYLAAA
GVGTIGIIDA DVVDDSNLQR QILHNTQRIG QYKAESARET IEALNPDVKV ITHIERLDES
NVARIIADYD VILDGTDNFP TRYLLNDAAL IANKPVVHGS VFRFEGQLTV FKPYEGPCYR
CLYPEPPPMA LAPSCAEAGV LGVLPGIIGI LQATETIKLL LGIGDPLVGR MMTYDALAGE
FNELRLFRDP KCAACGENGH PENLPTYADV CAIPA
//
