ID J7IYR9_DESMD Unreviewed; 870 AA.
AC J7IYR9;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Selenium-dependent molybdenum hydroxylase 1 {ECO:0000313|EMBL:AFQ43821.1};
GN OrderedLocusNames=Desmer_1863 {ECO:0000313|EMBL:AFQ43821.1};
OS Desulfosporosinus meridiei (strain ATCC BAA-275 / DSM 13257 / KCTC 12902 /
OS NCIMB 13706 / S10).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=768704 {ECO:0000313|EMBL:AFQ43821.1, ECO:0000313|Proteomes:UP000005262};
RN [1] {ECO:0000313|EMBL:AFQ43821.1, ECO:0000313|Proteomes:UP000005262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-275 / DSM 13257 / NCIMB 13706 / S10
RC {ECO:0000313|Proteomes:UP000005262};
RX PubMed=23105050; DOI=10.1128/JB.01392-12;
RA Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA Ollivier B., Klenk H.P., Spring S., Loy A.;
RT "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT and Desulfosporosinus acidiphilus DSM22704T.";
RL J. Bacteriol. 194:6300-6301(2012).
RN [2] {ECO:0000313|Proteomes:UP000005262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-275 / DSM 13257 / NCIMB 13706 / S10
RC {ECO:0000313|Proteomes:UP000005262};
RA Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Tapia R., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Peters L., Pitluck S., Woyke T., Pester M., Spring S., Ollivier B.,
RA Rattei T., Klenk H.-P., Wagner M., Loy A.;
RT "Finished genome of Desulfosporosinus meridiei DSM 13257.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|ARBA:ARBA00001927};
CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC iron-sulfur protein family. {ECO:0000256|ARBA:ARBA00009433}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006849}.
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DR EMBL; CP003629; AFQ43821.1; -; Genomic_DNA.
DR RefSeq; WP_014902736.1; NC_018515.1.
DR AlphaFoldDB; J7IYR9; -.
DR STRING; 768704.Desmer_1863; -.
DR KEGG; dmi:Desmer_1863; -.
DR eggNOG; COG1529; Bacteria.
DR eggNOG; COG2080; Bacteria.
DR HOGENOM; CLU_001681_2_3_9; -.
DR OrthoDB; 9759099at2; -.
DR Proteomes; UP000005262; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 5.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR025192; Succ_DH/fum_Rdtase_N.
DR InterPro; IPR017697; Xdh.
DR NCBIfam; TIGR03311; Se_dep_XDH; 1.
DR PANTHER; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 1.
DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR Pfam; PF13085; Fer2_3; 1.
DR Pfam; PF02738; MoCoBD_1; 1.
DR Pfam; PF20256; MoCoBD_2; 2.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..74
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 870 AA; 93768 MW; 249E6D900773D399 CRC64;
MFIVNINGKD YQSETDLSLM DFLRDELQIT SVKNGCKEGA CGTCTVIIDG KTVRACVQKL
SKLAGKKIQT IEGFTERERQ VFGYAFAASG AVQCGFCIPG MVISGKSLLD RNPDPTREDV
KGSIRTNICR CTGYSKIEDG ILLAAKMLRE NLEIPEMVQT GKVGEKTCRV DALPKTLGTA
MYADDFSFPG MLYGKNVFSK FARAKILAID LSKALIMPGV VAIYTAKDIP GQRYIGHLAQ
DWPGMIDVGE QTKCCGDTLA MVVAETREQA MAAVKAVEVQ YEPLNPICTP QEAAVPDAHQ
IHGEGFWQFG KFRIPENNLF DHEEVKRGDA ETALRNAKFV VEGTFQLPPT EHAFMEPETA
VALPDGDGVK VITGGQGIYD EYHEISAYLG LPLEKVRIQS AVVGGGFGGK EDMSVQHQAA
LCAYLTKRPV KVAFSRQESI NYHPKRHAME IYCKIGCDEK GILQGMQARI TSDTGAYASL
GGPVLQRACT HAGGPYNYQN VDIEGNAYYT NNPPAGAFRG FGVTQSCAVV ECLINQLAEK
AGISGWEIRY RNAIRPGQSL PNGQIADEGT AMAETLAAVK EEFEKYEADP DYYVGIASAM
KNAGVGVGVP DIGRCNLKII GGKVHARSSA GAIGQGIQTV LTQVICDTTG LLTNQVVVEH
PDTKYTPDSG TTTASRQTVF AGEAARQSAL QLKAELDTGK SLADLEGNEY IGEFEFKTDP
IGSPKPNPVS HVAYGYATQL FILDKEGKVV KVIAAHDVGR AINPLSAGGQ VEGGVAMGLG
YALTEDFPLK DGIPQAKLGT LGLFKAPQMP PVEVHLLGKN SPEIAFGAKG VGEIVCVMGA
PACQNAYYKK DGVFRYKYPL ENTYYRKPKA
//
