ID A0A0K1ELR7_CHOCO Unreviewed; 647 AA.
AC A0A0K1ELR7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Aldehyde ferredoxin oxidoreductase {ECO:0000313|EMBL:AKT41845.1};
GN ORFNames=CMC5_060560 {ECO:0000313|EMBL:AKT41845.1};
OS Chondromyces crocatus.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae;
OC Chondromyces.
OX NCBI_TaxID=52 {ECO:0000313|EMBL:AKT41845.1, ECO:0000313|Proteomes:UP000067626};
RN [1] {ECO:0000313|EMBL:AKT41845.1, ECO:0000313|Proteomes:UP000067626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cm c5 {ECO:0000313|EMBL:AKT41845.1,
RC ECO:0000313|Proteomes:UP000067626};
RA Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals a
RT high potential for natural compound synthesis and the genetic basis for the
RT loss of fruiting body formation.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the AOR/FOR family.
CC {ECO:0000256|ARBA:ARBA00011032}.
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; CP012159; AKT41845.1; -; Genomic_DNA.
DR RefSeq; WP_063796372.1; NZ_CP012159.1.
DR AlphaFoldDB; A0A0K1ELR7; -.
DR STRING; 52.CMC5_060560; -.
DR KEGG; ccro:CMC5_060560; -.
DR PATRIC; fig|52.7.peg.6666; -.
DR Proteomes; UP000067626; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016625; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor; IEA:InterPro.
DR Gene3D; 1.10.569.10; Aldehyde Ferredoxin Oxidoreductase Protein, subunit A, domain 2; 1.
DR Gene3D; 1.10.599.10; Aldehyde Ferredoxin Oxidoreductase Protein, subunit A, domain 3; 1.
DR Gene3D; 3.60.9.10; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 1.
DR InterPro; IPR013984; Ald_Fedxn_OxRdtase_dom2.
DR InterPro; IPR013985; Ald_Fedxn_OxRdtase_dom3.
DR InterPro; IPR013983; Ald_Fedxn_OxRdtase_N.
DR InterPro; IPR036503; Ald_Fedxn_OxRdtase_N_sf.
DR InterPro; IPR001203; OxRdtase_Ald_Fedxn_C.
DR InterPro; IPR036021; Tungsten_al_ferr_oxy-like_C.
DR PANTHER; PTHR30038; ALDEHYDE FERREDOXIN OXIDOREDUCTASE; 1.
DR PANTHER; PTHR30038:SF7; TUNGSTEN-CONTAINING GLYCERALDEHYDE-3-PHOSPHATE:FERREDOXIN OXIDOREDUCTASE; 1.
DR Pfam; PF01314; AFOR_C; 1.
DR Pfam; PF02730; AFOR_N; 1.
DR SMART; SM00790; AFOR_N; 1.
DR SUPFAM; SSF48310; Aldehyde ferredoxin oxidoreductase, C-terminal domains; 1.
DR SUPFAM; SSF56228; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000067626}.
FT DOMAIN 18..220
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
FT REGION 625..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 647 AA; 68668 MW; 55DDAF4AFEC153F0 CRC64;
MPPSLPAAHT PHLPTGGWFG RYLRIDLSRR STEVVEIEPR VSRQLIGGVG LGTWLLTQET
KAGFDPLGEE AALVVAFGPL VGTPLTTSAK VAFVAKSPLT GRLNDALSSS GFAIAGKRTG
FDALVLRGRA AEPSVVLTDG DALEVVPCPA LWGQALRLGE LEARLAAQFP GYELTIAGIA
AEHRVRYASL ANNGRHAGRG GLGAVLAAKQ IKAVGVRGCH AVPLAHAERA VTLARDLARR
SLGPATEKYR ELGTVANLAT FNRLAALPTR NFQESTFEGA TALSGESLRE TRARGRSACS
GCTIGCEHFF EVTPGAPPVK AEYENVFALG PLCGVSSPEL VLRASRLCDE LGLDTISAGG
SIAFAMECAE RGVFAGTQWE AEAKGLRFGD GARMLELLEA IAHRRAGLGA LLAEGSRRAA
EILGPPAPGF AAHVKGLEIP GYEPRALQTM ALGFAVSSRG ADHNRSGAYE VDFSGRVDRL
AGSPEAARLA VETEDRAAVL DSLILCKFLR RALRDVHEEA AEMLTAVTGA PVDMPEVQSA
AKRIVLLKRL FNEREGWRPE EDTLPARFFE ELLPGGAARG AGLTREQFEE MKRAYHEARG
LNADGSLPRA TIEEFGLDAL LTGRNADTLD APGMHPARGA RGEPEDR
//