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Database: UniProt
Entry: A0A0K1ELR7_CHOCO
LinkDB: A0A0K1ELR7_CHOCO
Original site: A0A0K1ELR7_CHOCO 
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}.
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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
//
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