ID A8GCK6_SERP5 Unreviewed; 367 AA.
AC A8GCK6;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=MOSC domain containing protein {ECO:0000313|EMBL:ABV40846.1};
GN OrderedLocusNames=Spro_1742 {ECO:0000313|EMBL:ABV40846.1};
OS Serratia proteamaculans (strain 568).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741 {ECO:0000313|EMBL:ABV40846.1};
RN [1] {ECO:0000313|EMBL:ABV40846.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568 {ECO:0000313|EMBL:ABV40846.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000826; ABV40846.1; -; Genomic_DNA.
DR AlphaFoldDB; A8GCK6; -.
DR STRING; 399741.Spro_1742; -.
DR KEGG; spe:Spro_1742; -.
DR eggNOG; COG1018; Bacteria.
DR eggNOG; COG3217; Bacteria.
DR HOGENOM; CLU_028286_0_2_6; -.
DR OrthoDB; 581532at2; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR005303; MOCOS_middle.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR PANTHER; PTHR36930; METAL-SULFUR CLUSTER BIOSYNTHESIS PROTEINS YUAD-RELATED; 1.
DR PANTHER; PTHR36930:SF1; MOSC DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF141673; MOSC N-terminal domain-like; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027}.
FT DOMAIN 120..263
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT DOMAIN 288..367
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 367 AA; 40072 MW; BAEB66F6226ED8CA CRC64;
MITLAKLYVH PVKSLRGLQL SHAQVSSSGL AFDRTFMITE PDGTFITARQ YPQMVLFTPA
LLADGLFLTA PDGESAAIRF SDFAAEAQPT EVWGNHFTAL IAPQAINSWL SGYFQRDVQL
RWLGPELTRR VKKHPEIPLS FADGYPYLLI NEASFNDLQQ RCPGSIKLEQ FRPNLVVTGA
SAWAEDGWQV IRVGDVMFDL VKPCSRCVLT TVSIERGRKH PSGEPLSTLQ KFRTADNGDV
DFGQNMVARN SGIIRVGDAV EVLSTKPPRP YGAGKVVESV QAPQDSAQNV TIDYAGTVFT
GNNQQILLEQ LEQQGLRVPY SCRAGICGSC RITLVNGEVA PLKKSAVANN GTILCCSCIP
KSDLTLA
//