ID Q64V50_BACFR Unreviewed; 426 AA.
AC Q64V50;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Putative coproporphyrinogen III oxidase and related FeS oxidoreductase {ECO:0000313|EMBL:BAD48628.1};
GN OrderedLocusNames=BF1880 {ECO:0000313|EMBL:BAD48628.1};
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405 {ECO:0000313|EMBL:BAD48628.1, ECO:0000313|Proteomes:UP000002197};
RN [1] {ECO:0000313|EMBL:BAD48628.1, ECO:0000313|Proteomes:UP000002197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46 {ECO:0000313|EMBL:BAD48628.1,
RC ECO:0000313|Proteomes:UP000002197};
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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DR EMBL; AP006841; BAD48628.1; -; Genomic_DNA.
DR RefSeq; WP_011202627.1; NC_006347.1.
DR RefSeq; YP_099162.1; NC_006347.1.
DR AlphaFoldDB; Q64V50; -.
DR STRING; 295405.BF1880; -.
DR KEGG; bfr:BF1880; -.
DR PATRIC; fig|295405.11.peg.1830; -.
DR HOGENOM; CLU_027579_7_1_10; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000002197; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR010723; HemN_C.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR13932; COPROPORPHYRINIGEN III OXIDASE; 1.
DR PANTHER; PTHR13932:SF5; RADICAL S-ADENOSYL METHIONINE DOMAIN-CONTAINING PROTEIN 1, MITOCHONDRIAL; 1.
DR Pfam; PF06969; HemN_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01065; anaerobic_coproporphyrinogen-I; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 38..272
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 426 AA; 48783 MW; F81CE37DF07C32F8 CRC64;
MNEQQQISRY VSYMYSYPHK TAYRTLTPPV SLSPYLERLE GREASLYFHI PFCAHKCGYC
NLFSQQCCDA ERISLYLHTM RRQAEQLSVA AQGLKFTSFA VGGGTPLILD EGQLEELFCL
AELFGVHPSR VFTSVETSPE YTQKSVLRQL RARGVERLSM GVQSFNETEL KKLKRRPGLG
TVVGALENIV EAGFPQFNLD LIYGIEGQTV ESFMRSLNTA LTYRPNELFI YPLYVRPGTR
INVRSTDDIG YAIYKSAREL LVGQGFVQTS MRRFVRRETT ETEFSCGDEV MLSCGAGGRS
YLGNLHYATP YAVRQQAIAD EIDHYIRTTD FMTAANGFLL STEEMQIRFI IKNLMYHRGV
DLAEYEKRFG EKPDRNLFRE FTDRGWIEET GRIVRLTEEG MAYSDYIGQA FISPAVRKLM
SEYVYP
//
