GenomeNet

Database: UniProt
Entry: A0A200H7Y4_9ACTN
LinkDB: A0A200H7Y4_9ACTN
Original site: A0A200H7Y4_9ACTN 
ID   A0A200H7Y4_9ACTN        Unreviewed;       249 AA.
AC   A0A200H7Y4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:OUZ08551.1};
GN   ORFNames=BHE97_12785 {ECO:0000313|EMBL:OUZ08551.1};
OS   Aeromicrobium sp. PE09-221.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=1898043 {ECO:0000313|EMBL:OUZ08551.1, ECO:0000313|Proteomes:UP000195423};
RN   [1] {ECO:0000313|EMBL:OUZ08551.1, ECO:0000313|Proteomes:UP000195423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PE09-221 {ECO:0000313|EMBL:OUZ08551.1,
RC   ECO:0000313|Proteomes:UP000195423};
RX   PubMed=28218694;
RA   Matobole R.M., van Zyl L.J., Parker-Nance S., Davies-Coleman M.T.,
RA   Trindade M.;
RT   "Antibacterial Activities of Bacteria Isolated from the Marine Sponges
RT   Isodictya compressa and Higginsia bidentifera Collected from Algoa Bay,
RT   South Africa.";
RL   Mar. Drugs 15:E47-E47(2017).
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   -!- 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:OUZ08551.1}.
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; MIJB01000024; OUZ08551.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A200H7Y4; -.
DR   OrthoDB; 9804391at2; -.
DR   Proteomes; UP000195423; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR025192; Succ_DH/fum_Rdtase_N.
DR   PANTHER; PTHR11921:SF41; 4FE-4S FERREDOXIN IRON-SULFUR BINDING DOMAIN PROTEIN; 1.
DR   PANTHER; PTHR11921; SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN; 1.
DR   Pfam; PF13085; Fer2_3; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
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:UP000195423}.
FT   DOMAIN          149..179
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   249 AA;  26463 MW;  4842460597D56E61 CRC64;
     MKITVRIWRQ KGPEAKGTMV PYELDDVSEH MSFLEMLDVL NERLTLEGEE PVAFDSDCRE
     GICGMCGVVI NGIAHGPEVT TTCQLHMRTF NDGDTIDIEP WRAGAFPVVK DLVVDRGAFD
     RIIAAGGYIT APTGSAPEAN NLPVPKIDAD HAFEAATCIG CGACVAACPN GSAMLFTAAK
     ITHLGLLPQG QPERESRVLN MVEQMDAEGF GSCTNIGECT AACPKGIPLD VISQLNRDLM
     GALAKPGSA
//
DBGET integrated database retrieval system